site of glutaminesynthetase illuminates the mechanism of enzymatic inhibition journal Biochemistry ... url issn ref Pfam box Symbol Gln synt N Name Glutaminesynthetase, br beta Grasp domain image width 150 caption Crystallographic structure of glutaminesynthetase from salmonella typhimurium . ref name ... 2qc8 , PDB2 2ojw Pfam box Symbol Gln synt C Name Glutaminesynthetase, br catalytic domain image PDB 2gls EBI.jpg width caption 12 subunit enzyme glutaminesynthetase from Salmonella typhimurium . ref ... D title Refined atomic model of glutaminesynthetase at 3.5 A resolution journal J. Biol. Chem ... , PDB2 2ojw protein Name glutamate ammonia ligase glutaminesynthetase caption image width HGNCid ... ECnumber 6.3.1.2 Chromosome 1 Arm q Band 31 LocusSupplementaryData stack end Glutaminesynthetase ... catalysts glutaminesynthetase and RuBisCO journal Cold Spring Harb. Symp. Quant. Biol. volume 52 issue ... Image GS reacction.PNG center alt GlutamineSynthetase reaction. GlutamineSynthetase Catalyzed Reaction. GlutamineSynthetase uses ammonia produced by nitrate reduction, amino acid degradation, and photorespiration ... of the ammonium substrate site on glutaminesynthetase, a third cation binding site journal Protein ... Feedback inhibition of fully unadenylylated glutaminesynthetase from Salmonella typhimurium by glycine ... model for the reaction mechanism of glutaminesynthetase, based on five crystal structures ... left alt GS Dodecamer GlutamineSynthetase 12 subunits. ref name pmid11329256 GlutamineSynthetase can ... title GlutamineSynthetase author Goodsell DS date 2002 06 work Molecule of the month publisher RCSB ... properties of the glutaminesynthetase from Escherichia coli journal Biochemistry volume 9 issue ... Feedback inhibition of fully unadenylylated glutaminesynthetase from Salmonella typhimurium by glycine ... A, Stadtman ER title Metal ion requirement by glutaminesynthetase of Escherichia coli in catalysis ... GlutamineSynthetase author Goodsell, DS date June 2002 work publisher RCSB Protein Data Bank accessdate ... more details
Infobox protein family Symbol GATase Name Glutamine amidotransferase class I image PDB 1o1y EBI.jpg width caption crystal structure of putative glutamine amido transferase tm1158 from thermotoga maritima at 1.70 a resolution Pfam PF00117 Pfam clan CL0014 InterPro IPR000991 SMART PROSITE PDOC00406 MEROPS C44 SCOP 1ea0 TCDB OPM family OPM protein CAZy CDD In molecular biology, glutamine amidotransferases GATase are enzymes which catalyse the removal of the ammonia group from a glutamic acid glutamate molecule and its subsequent transfer to a specific substrate, thus creating a new carbon nitrogen group on the Enzyme substrate substrate . This activity is found in a range of biosynthetic enzymes, including glutamine amidotransferase, anthranilate synthase component II, p aminobenzoate, and glutamine dependent carbamoyl transferase CPSase . Glutamine amidotransferase GATase protein domain domains can occur either as single polypeptides, as in glutamine amidotransferases, or as protein domains domains in a much larger multifunctional synthase protein, such as CPSase. On the basis of sequence biology sequence similarities two classes of GATase domains have been identified class I also known as trpG type and class II also known as purF type ref name pmid3298209 cite journal author Weng ML, Zalkin H title Structural role for a conserved region in the CTP synthetaseglutamine amide transfer domain journal J. Bacteriol. volume 169 issue 7 pages 3023 8 year 1987 month July pmid 3298209 pmc 212343 doi url ref ref name pmid6086650 cite journal author Nyunoya H, Lusty CJ title Sequence of the small subunit of yeast carbamyl phosphate synthetase and identification of its catalytic domain journal J. Biol. Chem. volume 259 issue 15 pages 9790 8 year 1984 month August pmid 6086650 doi url ref . Class I GATase domains are defined by a conserved sequence conserved catalytic triad consisting ... synthase GMP synthase glutamine dependent carbamoyl phosphate synthase phosphoribosylformylglycinamidine ... more details
protein Name asparagine synthetase caption image width HGNCid 753 Symbol ASNS AltSymbols EntrezGene 440 OMIM 108370 RefSeq NM 001673 UniProt P08243 PDB ECnumber 6.3.5.4 Chromosome 7 Arm q Band 21 LocusSupplementaryData q31 Asparagine synthetase or aspartate ammonia ligase is an enzyme that generates asparagine from aspartate . This amidation reaction is similar to that promoted by glutaminesynthetase . External links MeshName Asparagine synthetase ligase stub Ligases Amino acid metabolism enzymes de Asparaginsynthetase ja ... more details
protein Name holocarboxylase synthetase biotin proprionyl Coenzyme A carboxylase ATP hydrolysing ligase caption image width HGNCid 4976 Symbol HLCS AltSymbols EntrezGene 3141 OMIM 609018 RefSeq NM 000411 UniProt P50747 PDB ECnumber 6.3.4.10 Chromosome 21 Arm q Band 22.1 LocusSupplementaryData HLCS holocarboxylase synthetase biotin proprionyl Coenzyme A carboxylase ATP hydrolysing ligase is a human gene that provides instructions for making an enzyme called holocarboxylase synthetase EC number 6.3.4.10 . This enzyme is important for the effective use of biotin , a B vitamin found in foods such as liver , egg yolk s, and milk . In many of the body s tissues, holocarboxylase synthetase activates other specific enzymes called biotin dependent carboxylases by attaching biotin to them. These carboxylases are involved in many critical cellular functions, including the production and breakdown of proteins, fats, and carbohydrates. Holocarboxylase synthetase may also play a role in regulating the activity of genes. In the nucleus, the enzyme likely attaches biotin molecules to histones, which are structural proteins that bind to DNA and give chromosomes their shape. Changing the shape of histones may help determine whether certain genes are turned on or off however, it is not known how adding biotin affects gene regulation. The HLCS gene is located on the long q arm of chromosome 21 human chromosome 21 at position 22.1, from base pair 37,045,059 to base pair 37,284,372. Related conditions Holocarboxylase synthetase deficiency About 30 mutation s in the HLCS gene have been identified in people with holocarboxylase synthetase deficiency. Most of these mutations substitute one amino acid a building block of proteins for another amino acid in the holocarboxylase synthetase enzyme. Many ... synthetase activity may also alter the regulation of certain genes that are important for normal ... synthetase deficiency. See also Biotinylation External links MeshName holocarboxylase synthetases Ligases ... more details
protein Name glutathione synthetase caption image width HGNCid 4624 Symbol GSS AltSymbols EntrezGene 2937 OMIM 601002 RefSeq NM 000178 UniProt P48637 PDB ECnumber 6.3.2.3 Chromosome 20 Arm q Band 11.2 LocusSupplementaryData Infobox protein family Symbol GSH synthase Name Eukaryotic glutathione synthase image PDB 2hgs EBI.jpg width caption human glutathione synthetase Pfam PF03199 Pfam clan CL0483 InterPro IPR004887 SMART PROSITE MEROPS SCOP 2hgs TCDB OPM family OPM protein CAZy CDD Infobox protein family Symbol GSH synth ATP Name Eukaryotic glutathione synthase, ATP binding domain image PDB 2hgs EBI.jpg width caption human glutathione synthetase Pfam PF03917 Pfam clan InterPro IPR005615 SMART PROSITE MEROPS SCOP 1m0t TCDB OPM family OPM protein CAZy CDD Infobox protein family Symbol GSH S N Name Prokaryotic glutathione synthetase, N terminal domain image PDB 1gsh EBI.jpg width caption structure of escherichia coli glutathione synthetase at ph 7.5 Pfam PF02951 Pfam clan InterPro IPR004215 SMART PROSITE MEROPS SCOP 1glv TCDB OPM family OPM protein CAZy CDD Infobox protein family Symbol GSH S ATP Name Prokaryotic glutathione synthetase, ATP grasp domain image PDB 1gsh EBI.jpg width caption structure of escherichia coli glutathione synthetase at ph 7.5 Pfam PF02955 Pfam clan CL0179 InterPro IPR004218 SMART PROSITE MEROPS SCOP 1glv TCDB OPM family OPM protein CAZy CDD Glutathione synthetase GSS EC 6.3.2.3 is the second enzyme in the glutathione biosynthesis pathway. It catalyses the condensation of gamma glutamylcysteine and glycine , to form glutathione. ref cite journal author Nj lsson R, Norgren S title Physiological and pathological aspects of GSH metabolism. journal Acta Paediatr volume 94 issue 2 pages 132 7 year 2005 pmid 15981742 doi 10.1080 08035250410025285 ref In eukaryotes ... Polekhina G, Board PG, Gali RR, Rossjohn J, Parker MW title Molecular basis of glutathione synthetase ... synthetase deficiency References references External links MeshName Glutathione Synthetase ligase ... more details
enzyme Name N 5 amino 5 carboxypentanoyl small L small cysteinyl small D small valine synthase EC number 6.3.2.26 CAS number 57219 73 5 IUBMB EC number 6 3 2 26 GO code 0050564 image width caption ACV synthetase ACVS , small L small aminoadipoyl small L small cysteinyl small D small valine synthetase , N 5 amino 5 carboxypentanoyl small L small cysteinyl small D small valine synthase , EC number 6.3.2.26 is an enzyme that catalysis catalyzes the chemical reaction 3 ATP small L small 2 aminohexanedioate small L small cysteine small L small valine H sub 2 sub O math rightleftharpoons math 3 AMP 3 PP sub i sub N small L small 5 amino 5 carboxypentanoyl small L small cysteinyl small D small valine The five substrate biochemistry substrates of this enzyme are adenosine triphosphate ATP , small L small 2 aminohexanedioate, small L small cysteine , small L small valine , and water H sub 2 sub O , whereas its three product chemistry products are adenosine monophosphate AMP , diphosphate , and N small L small 5 amino 5 carboxypentanoyl small L small cysteinyl small D small valine. ACVS is an example of a Nonribosomal peptide nonribosomal peptide synthetase NRPS . It participates in penicillin and cephalosporin biosyntheses. References reflist 1 cite journal author Byford MF, Baldwin JE, Shiau CY, Schofield CJ date 1997 title The Mechanism of ACV Synthetase journal Chem. Rev. volume 97 pages 2631&ndash 2650 pmid 11851475 doi 10.1021 cr960018l issue 7 cite journal author Theilgaard HB, Kristiansen KN, Henriksen CM, Nielsen J date Pt 1 title Purification and characterization of delta L alpha aminoadipyl L cysteinyl D valine synthetase from Penicillium chrysogenum journal Biochem. J. volume 327 pages 185&ndash 91 pmid 9355751 pmc 1218779 ligase stub Category EC 6.3.2 Category Enzymes of unknown structure ... more details
Expert subject Molecular and Cellular Biology date January 2009 Human phosphopantothenoylcysteine synthetase PPC synthetase is a dimer with identical monomers. PPC syththetase converts phosphopantothenate into phosphopantothenoylcysteine by combining with cysteine while using a unit of ATP. References reflist Cite journal doi 10.1016 S0969 2126 03 00146 1 journal Structure year 2003 month Aug volume 11 issue 8 pages 927 936 title Structure of human phosphopantothenoylcysteine synthetase at 2.3 A resolution author Manoj N, Strauss E, Begley TP, Ealick SE pmid 12906824 cite journal journal DNA Repair Amst year 2003 month May volume 13 2 issue 5 pages 441 53 title The enigma of endonuclease VIII author Wallace SS, Bandaru V, Kathe SD, Bond JP url http www.hprd.org alternate?protein 07760&isoform id 07760 1&isoform name Isoform 1 doi 10.1016 S1568 7864 02 00182 9 enzyme stub Category Enzymes ... more details
enzyme Name Phosphoribosylaminoimidazole synthetase EC number 2.1.2.2 CAS number 9032 02 4 IUBMB EC number 2 1 2 2 GO code 0004644 image width caption In the field of enzymology , phosphoribosylaminoimidazole synthetase is an enzyme that catalyzes the chemical reaction 10 formyltetrahydrofolate N1 5 phospho D ribosyl glycinamide math rightleftharpoons math tetrahydrofolic acid tetrahydrofolate N2 formyl N1 5 phospho D ribosyl glycinamide This enzyme is required for the de novo biosynthesis of purine s. References refbegin cite journal author Hartman SC, Buchanan JM title Biosynthesis of the purines. XXVI. The identification of the formyl donors of the transformylation reactions journal J. Biol. Chem. volume 234 issue 7 pages 1812 6 year 1959 month July pmid 13672969 doi url issn cite journal author Smith GK, Benkovic PA, Benkovic SJ title L 10 Formyltetrahydrofolate is the cofactor for glycinamide ribonucleotide transformylase from chicken liver journal Biochemistry volume 20 issue 14 pages 4034 6 year 1981 month July pmid 7284307 doi 10.1021 bi00517a013 url issn cite journal author Warren L, Buchanan JM title Biosynthesis of the purines. XIX. 2 Amino N ribosylacetamide 5 phosphate glycinamide ribotide transformylase journal J. Biol. Chem. volume 229 issue 2 pages 613 26 year 1957 month December pmid 13502326 doi url issn refend transferase stub Category EC 2.1.2 ja ... more details
enzyme Name glutamine tRNA ligase EC number 6.1.1.18 CAS number 9075 59 6 IUBMB EC number 6 1 1 18 GO code 0004819 image width caption In enzymology , a glutamine tRNA ligase EC number 6.1.1.18 is an enzyme that catalysis catalyzes the chemical reaction ATP L glutamine tRNAGln math rightleftharpoons math AMP diphosphate L glutaminyl tRNAGln The 3 substrate biochemistry substrates of this enzyme are adenosine triphosphate ATP , L glutamine , and tRNA Gln , whereas its 3 product chemistry products are adenosine monophosphate AMP , diphosphate , and L glutaminyl tRNA Gln . This enzyme belongs to the family of ligase s, to be specific those forming carbon oxygen bonds in aminoacyl tRNA and related compounds. The systematic name of this enzyme class is L glutamine tRNAGln ligase AMP forming . Other names in common use include glutaminyl tRNA synthetase , glutaminyl transfer RNA synthetase , glutaminyl transfer ribonucleate synthetase , glutamine tRNA synthetase , glutamine translase , glutamate tRNA ligase , glutaminyl ribonucleic acid , and GlnRS . This enzyme participates in glutamate metabolism and aminoacyl trna biosynthesis . Structural studies As of late 2007, 15 tertiary structure structures have been solved for this class of enzymes, with Protein Data Bank PDB accession codes PDB link 1EUQ , PDB link 1EUY , PDB link 1EXD , PDB link 1GSG , PDB link 1GTR , PDB link 1GTS , PDB link 1NYL , PDB link 1O0B , PDB link 1O0C , PDB link 1QRS , PDB link 1QRT , PDB link 1QRU , PDB link 1QTQ , PDB link 1ZJW , and PDB link 2HZ7 . References reflist 1 cite journal author Ravel JM, Wang S, Heinemeyer C and Shive W year 1965 title Glutamyl and glutaminyl ribonucleic acid synthetases of Escherichia coli W. Separation, properties, and stimulation of adenosine triphosphate pyrophosphate exchange by acceptor ribonucleic acid journal J. Biol. Chem. volume 240 pages 432&ndash 438 pmid 14253448 Ligases Category EC 6.1.1 Category Enzymes of known structure ligase stub ... more details
Orphan date February 2009 Glutamine oxoglutarate aminotransferase also known as Glutamate synthase is an enzyme and frequently abbreviated as GOGAT . This enzyme manufactures glutamate from glutamine and ketoglutarate , and thus along with glutaminesynthetase abbreviated GS plays a central role in the regulation of nitrogen assimilation in photosynthetic eukaryotes and prokaryotes. ref name Zadykowicz Phylogenetic Relationships Among Glutamate Synthase GOGAT Enzymes Eva Zadykowicz and Deborah L. Robertson Department of Biology, Clark University, Worcester, MA ref ref name Keiser Practical Streptomyces Genetics Keiser et al John Innes Foundation, Norwich, England ref This is of great importance as primary productivity in many marine environments is regulated by the availability of inorganic nitrogen. The primary sources of inorganic nitrogen used by marine algae are nitrate and ammonium . Both forms are ultimately incorporated into amino acids through the sequential reaction of glutaminesynthetase GS and glutamate synthase glutamine 2 oxyoglutarate aminotransferase GOGAT . GOGAT isoenzymes catalyze the transfer of the amido nitrogen of glutamine to 2 oxoglutarate using pyridine nucleotides NADH NADPH dependent or ferredoxin Fd dependent as reductants. ref name Zadykowicz In photosynthetic eukaryotes, GS and GOGAT isoenzymes are localized in the cytosol and chloroplast . Fd GOGAT is found strictly in cyanobacteria and photosynthetic eukaryotes, and the gene is located in the chloroplast of rhodophytes and in the nucleus of vascular plants, but in both cases its product is active in the chloroplast. NADH GOGAT is found in the nucleus of vascular plants, fungi, and diatoms, while NADPH GOGAT is found in non photosynthetic bacteria and archaea. ref name Zadykowicz References reflist DEFAULTSORT Glutamine Oxoglutarate Aminotransferase Category Enzymes cell biology stub ... more details
enzyme Name NAD synthase glutamine hydrolyzing EC number 6.3.5.1 CAS number 37318 70 0 IUBMB EC number 6 3 5 1 GO code 0003952 image width caption In enzymology , a NAD synthase glutamine hydrolysing EC number 6.3.5.1 is an enzyme that catalysis catalyzes the chemical reaction ATP deamido NAD sup sup L glutamine H sub 2 sub O math rightleftharpoons math AMP diphosphate NAD sup sup L glutamate The 4 substrate biochemistry substrates of this enzyme are adenosine triphosphate ATP , deamido NAD , L glutamine , and water H sub 2 sub O , whereas its 4 product chemistry products are adenosine monophosphate AMP , diphosphate , nicotinamide adenine dinucleotide NAD sup sup , and L glutamate . This enzyme belongs to the family of ligase s, specifically those forming carbon nitrogen bonds carbon nitrogen ligases with glutamine as amido N donor. The systematic name of this enzyme class is deamido NAD L glutamine amido ligase AMP forming . Other names in common use include NAD synthetaseglutamine hydrolysing , nicotinamide adenine dinucleotide synthetaseglutamine , desamidonicotinamide adenine dinucleotide amidotransferase , and DPN synthetase . This enzyme participates in glutamate metabolism and nicotinate and nicotinamide metabolism . Structural studies As of late 2007, 7 tertiary structure structures have been solved for this class of enzymes, with Protein Data Bank PDB accession codes PDB link 1EE1 , PDB link 1FYD , PDB link 1IFX , PDB link 1IH8 , PDB link 1KQP , PDB link 1NSY , and PDB link 2NSY . References reflist 1 cite journal author IMSANDE J date 1961 title Pathway of diphosphopyridine nucleotide biosynthesis in Escherichia coli journal J. Biol. Chem. volume 236 pages 1494&ndash 7 pmid 13717628 cite journal author IMSANDE J, HANDLER P date 1961 title Biosynthesis of diphosphopyridine nucleotide. III. Nicotinic acid mononucleotide pyrophos phorylase journal J. Biol. Chem. volume 236 pages 525&ndash 30 pmid 13717627 ligase stub Category EC 6.3.5 Category NADH dependent ... more details
In biochemistry , the glutamate glutamine cycle is a sequence of events by which an adequate supply of the neurotransmitter glutamate is maintained in the central nervous system . ref name Purves cite book author Purves, Dale, George J. Augustine, David Fitzpatrick, William C. Hall, Anthony Samuel LaMantia, James O. McNamara, and Leonard E. White title Neuroscience. 4th ed. publisher Sinauer Associates pages 128 9 year 2008 id ISBN 978 0 87893 697 7 ref Initially, glial cell s release glutamine , which is then taken up into presynaptic terminal s and metabolized into glutamate by glutaminase a mitochondria l enzyme . Glutamate can also be produced by transamination of 2 oxoglutarate , an intermediate in the Citric acid cycle . ref name Purves The glutamate that is synthesized in the presynaptic terminal is packaged into synaptic vesicle s by the transporter VGLUT . Once the vesicle is released, glutamate is removed from the synaptic cleft by excitatory amino acid transporter s EAATs , of which there are five types. Glutamate taken up by glial cells is then converted into glutamine by glutaminesynthetase , and transported out of the cells into the nerve terminal. This allows synaptic terminals and glial cells to work together in order to maintain a proper supply of glutamate. ref name Purves At GABAergic synapses, the cycle is called the GABA glutamine cycle. Here the glutamine taken up by neurons is converted to glutamate, which is then metabolized into GABA by glutamate decarboxylase . Upon release, GABA is taken up by glial cells via GABA transporters , metabolized into succinate, then in a series of steps to alpha ketoglutarate and then back to glutamine via glutamate. ref cite journal author Bak LK, Schousboe A, Waagepetersen HS title The glutamate GABA glutamine cycle aspects of transport, neurotransmitter homeostasis and ammonia transfer journal J. Neurochem. volume 98 issue 3 pages 641 53 year 2006 month August pmid 16787421 doi 10.1111 j.1471 4159.2006.03913.x ... more details
enzyme Name glutamine N phenylacetyltransferase EC number 2.3.1.14 CAS number 9030 00 6 IUBMB EC number 2 3 1 14 GO code 0047947 image width caption In enzymology , a glutamine N phenylacetyltransferase EC number 2.3.1.14 is an enzyme that catalysis catalyzes the chemical reaction phenylacetyl CoA L glutamine math rightleftharpoons math CoA alpha N phenylacetyl L glutamine Thus, the two substrate biochemistry substrates of this enzyme are phenylacetyl CoA and L glutamine , whereas its two product chemistry products are coenzyme A CoA and alpha N phenylacetyl L glutamine . This enzyme belongs to the family of transferase s, specifically those acyltransferase s transferring groups other than aminoacyl groups. The systematic name of this enzyme class is phenylacetyl CoA L glutamine alpha N phenylacetyltransferase . Other names in common use include glutamine phenylacetyltransferase , and phenylacetyl CoA L glutamine N acetyltransferase . This enzyme participates in tyrosine metabolism and phenylalanine metabolism . References reflist 1 cite journal author Moldave K and Meister A year 1957 title Synthesis of phenylacetylglutamine by human tissue journal J. Biol. Chem. volume 229 pages 463&ndash 476 pmid 13491597 issue 1 Category EC 2.3.1 Category Enzymes of unknown structure transferase stub it Glutammina N fenilacetiltransferasi ... more details
enzyme Name glutamine scyllo inositol transaminase EC number 2.6.1.50 CAS number 9033 03 8 IUBMB EC number 2 6 1 50 GO code 0047310 image width caption In enzymology , a glutamine scyllo inositol transaminase EC number 2.6.1.50 is an enzyme that catalysis catalyzes the chemical reaction L glutamine 2,4,6 3,5 pentahydroxycyclohexanone math rightleftharpoons math 2 oxoglutaramate 1 amino 1 deoxy scyllo inositol Thus, the two substrate biochemistry substrates of this enzyme are L glutamine and 2,4,6 3,5 pentahydroxycyclohexanone , whereas its two product chemistry products are 2 oxoglutaramate and 1 amino 1 deoxy scyllo inositol . This enzyme belongs to the family of transferase s, specifically the transaminases , which transfer nitrogenous groups. The systematic name of this enzyme class is L glutamine 2,4,6 3,5 pentahydroxycyclohexanone aminotransferase . Other names in common use include glutamine scyllo inosose aminotransferase , L glutamine keto scyllo inositol aminotransferase , glutamine scyllo inosose transaminase , and L glutamine scyllo inosose transaminase . It employs one cofactor biochemistry cofactor , pyridoxal phosphate . References reflist 1 cite journal author Walker JB, Walker MS date 1969 title Streptomycin biosynthesis. Transamination reactions involving inosamines and inosadiamines journal Biochemistry. volume 8 pages 763&ndash 70 pmid 5781017 doi 10.1021 bi00831a003 issue 3 transferase stub Category EC 2.6.1 Category Pyridoxal phosphate enzymes Category Enzymes of unknown structure ... more details
enzyme Name glutamine N acyltransferase EC number 2.3.1.68 CAS number 9030 00 6 IUBMB EC number 2 3 1 68 GO code 0047946 image width caption In enzymology , a glutamine N acyltransferase EC number 2.3.1.68 is an enzyme that catalysis catalyzes the chemical reaction acyl CoA L glutamine math rightleftharpoons math CoA N acyl L glutamine Thus, the two substrate biochemistry substrates of this enzyme are acyl CoA and L glutamine , whereas its two product chemistry products are coenzyme A CoA and N acyl L glutamine . This enzyme belongs to the family of transferase s, specifically those acyltransferase s transferring groups other than aminoacyl groups. The systematic name of this enzyme class is acyl CoA L glutamine N acyltransferase . References reflist 1 cite journal author Webster LT, Siddiqui UA, Lucas SV, Strong JM, Mieyal JJ date 1976 title Identification of separate acyl CoA glycine and acyl CoA L glutamine N acyltransferase activities in mitochondrial fractions from liver of rhesus monkey and man journal J. Biol. Chem. volume 251 pages 3352&ndash 8 pmid 931988 issue 11 transferase stub Category EC 2.3.1 Category Enzymes of unknown structure it Glutammina N aciltransferasi ... more details
of glutamine to form ammonia and glutamate ref James B. Thoden, et al. 1998 . Carbamoyl Phosphate Synthetase Caught in the Act of Glutamine Hydrolysis. Biochemistry 1998, 37, 8825 8831. http ...Protein Name carbamoyl phosphate synthetase 1, mitochondrial image caption Symbol CPS1 AltSymbols HGNCid ... Phosphate Synthetase I E.coli PDB 1jdb , EC number 6.3.5.5 is a ligase enzyme located in the mitochondria involved in the production of urea. Carbamoyl Phosphate Synthetase I CPSI transfers an ammonia from glutamine to a molecule of bicarbonate that has been phosphorylated by a molecule of ATP. The resulting ... phosphate leaves the enzyme. Structure of Carbamoyl Phosphate Synthetase I CPSI is a heterodimer ... name James James B. Thoden , Xinyi Hua, et al. Carbamoyl phosphate Synthetase Creation of an Escape ... and deamination of glutamine to make ammonia and glutamate. The large subunit contains ... phosphate ref name Sue SUE GLENN POWERS, Inhibition of Carbamyl Phosphate Synthetase by PI ... 10 3558 ref ref James B. Thoden, Hazel M. Holden, et al. 1997 . Structure of Carbamoyl Phosphate Synthetase ... in Carbamoyl Phosphate Synthetase Derails the Passage of Ammonia between Sequential Active Sites ... pubs.acs.org cgi bin article.cgi bichaw 2004 43 i18 pdf bi049945 .pdf ref . Image Glutamine complexed.jpg thumb right 200px Glutamine binding active site with Cys269 and His353 residues showing with glutamine ... Synthetase. Department of Chemistry, Texas A&M UniVersity, College Station, Texas 77843 http pubs.acs.org ... Synthetase I The overall reaction that occurs in CPSI is 2ATP HCO sub 3 sub sup sup NH sub 4 sub sup ... distinct steps ref name Alton . Bicarbonate is phosphorylated Ammonia is taken off glutamine The ammonia from glutamine attacks the carboxyphosphate, resulting in carbamate Carbamate is phosphorylated to give Carbamoyl phosphate Of these four steps, only step two the deamination of glutamine to get ... MICHAEL KOTH , BINNUR EROGLU, et al. Novel mechanism for carbamoyl phosphate synthetase A nucleotide ... more details
enzyme Name glutamine phenylpyruvate transaminase EC number 2.6.1.64 CAS number 68518 06 9 IUBMB EC number 2 6 1 64 GO code 0047316 image width caption In enzymology , a glutamine phenylpyruvate transaminase EC number 2.6.1.64 is an enzyme that catalysis catalyzes the chemical reaction L glutamine phenylpyruvate math rightleftharpoons math 2 oxoglutaramate L phenylalanine Thus, the two substrate biochemistry substrates of this enzyme are L glutamine and phenylpyruvate , whereas its two product chemistry products are 2 oxoglutaramate and L phenylalanine . This enzyme belongs to the family of transferase s, to be specific, the transaminases , that transfer nitrogenous groups. The systematic name of this enzyme class is L glutamine phenylpyruvate aminotransferase . Other names in common use include glutamine transaminase K , and glutamine phenylpyruvate aminotransferase . It employs one cofactor biochemistry cofactor , pyridoxal phosphate . Structural studies As of late 2007, two tertiary structure structures have been solved for this class of enzymes, with Protein Data Bank PDB accession codes PDB link 1YIY and PDB link 1YIZ . References reflist 1 cite journal author Cooper AJ date 1978 title Purification of soluble and mitochondrial glutamine transaminase K from rat kidney. Use of a sensitive assay involving transamination between L phenylalanine and alpha keto gamma methiolbutyrate journal Anal. Biochem. volume 89 pages 451&ndash 60 pmid 727444 doi 10.1016 0003 2697 78 90374 3 issue 2 cite journal author Cooper AJ, Meister A date 1974 title Isolation and properties of a new glutamine transaminase from rat kidney journal J. Biol. Chem. volume 249 pages 2554&ndash 61 pmid 4822504 issue 8 transferase stub Category EC 2.6.1 Category Pyridoxal phosphate enzymes Category Enzymes of known structure ... more details
enzyme Name glutamine pyruvate transaminase EC number 2.6.1.15 CAS number 9030 44 8 IUBMB EC number 2 6 1 15 GO code 0047945 image width caption In enzymology , a glutamine pyruvate transaminase EC number 2.6.1.15 is an enzyme that catalysis catalyzes the chemical reaction L glutamine pyruvate math rightleftharpoons math 2 oxoglutaramate L alanine Thus, the two substrate biochemistry substrates of this enzyme are L glutamine and pyruvate , whereas its two product chemistry products are 2 oxoglutaramate and L alanine . This enzyme belongs to the family of transferase s, specifically the transaminases , which transfer nitrogenous groups. The systematic name of this enzyme class is L glutamine pyruvate aminotransferase . Other names in common use include glutaminase II , L glutamine transaminase L , and glutamine oxo acid transaminase . This enzyme participates in glutamate metabolism . It employs one cofactor biochemistry cofactor , pyridoxal phosphate . Structural studies As of late 2007, 3 tertiary structure structures have been solved for this class of enzymes, with Protein Data Bank PDB accession codes PDB link 1V2D , PDB link 1V2E , and PDB link 1V2F . References reflist 1 cite journal author Cooper JL, Meister A date 1972 title Isolation and properties of highly purified glutamine transaminase journal Biochemistry. volume 11 pages 661&ndash 71 pmid 5059882 doi 10.1021 bi00755a001 issue 5 cite journal author MEISTER A date 1954 title Studies on the mechanism and specificity of the glutamine alpha keto acid transamination deamidation reaction journal J. Biol. Chem. volume 210 pages 17&ndash 35 pmid 13201566 issue 1 transferase stub Category EC 2.6.1 Category Pyridoxal phosphate enzymes Category Enzymes of known structure ... more details
enzyme Name protein glutamine glutaminase EC number 3.5.1.44 CAS number 62213 11 0 IUBMB EC number 3 5 1 44 GO code 0050568 image width caption In enzymology , a protein glutamine glutaminase EC number 3.5.1.44 is an enzyme that catalysis catalyzes the chemical reaction protein L glutamine H sub 2 sub O math rightleftharpoons math protein L glutamate NH sub 3 sub Thus, the two substrate biochemistry substrates of this enzyme are protein L glutamine and water H sub 2 sub O , whereas its two product chemistry products are protein L glutamate and ammonia NH sub 3 sub . This enzyme belongs to the family of hydrolase s, those acting on carbon nitrogen bonds other than peptide bonds, specifically in linear amides. The systematic name of this enzyme class is protein L glutamine amidohydrolase . Other names in common use include peptidoglutaminase II , glutaminyl peptide glutaminase , destabilase , and peptidylglutaminase II . References reflist 1 cite journal author Kikuchi M, Hayashida H, Nakano E, Sakaguchi K date 1971 title Peptidoglutaminase. Enzymes for selective deamidation of gamma amide of peptide bound glutamine journal Biochemistry. volume 10 pages 1222&ndash 9 pmid 4928623 doi 10.1021 bi00783a019 issue 7 hydrolase stub Category EC 3.5.1 Category Enzymes of unknown structure ... more details
enzyme Name glutamine fructose 6 phosphate transaminase isomerizing EC number 2.6.1.16 CAS number 9030 45 9 IUBMB EC number 2 6 1 16 GO code 0004360 image width caption In enzymology , a glutamine fructose 6 phosphate transaminase isomerizing EC number 2.6.1.16 is an enzyme that catalysis catalyzes the chemical reaction L glutamine D fructose 6 phosphate math rightleftharpoons math L glutamate D glucosamine 6 phosphate Thus, the two substrate biochemistry substrates of this enzyme are L glutamine and D fructose 6 phosphate , whereas its two product chemistry products are L glutamate and D glucosamine 6 phosphate . This enzyme belongs to the family of transferase s, specifically the transaminases , which transfer nitrogenous groups. The systematic name of this enzyme class is L glutamine D fructose 6 phosphate isomerase deaminating . Other names in common use include hexosephosphate aminotransferase , glucosamine 6 phosphate isomerase glutamine forming , glutamine fructose 6 phosphate transaminase isomerizing , D fructose 6 phosphate amidotransferase , glucosaminephosphate isomerase , glucosamine 6 phosphate synthase , and GlcN6P synthase . This enzyme participates in glutamate metabolism and aminosugars metabolism . Structural studies As of late 2007, 12 tertiary structure structures have been solved for this class of enzymes, with Protein Data Bank PDB accession codes PDB link 1JXA , PDB link 1MOQ , PDB link 1MOR , PDB link 1MOS , PDB link 1XFF , PDB link 1XFG , PDB link 2BPL , PDB link 2J6H , PDB link 2POC , PDB link 2PUT , PDB link 2PUV , and PDB link 2PUW . References reflist 1 cite journal author Ghosh S, Blumenthal HJ, Davidson E and Roseman S year 1960 title Glucosamine metabolism. V. Enzymatic synthesis of glucosamine 6 phosphate journal J. Biol. Chem. volume 235 pages 1265&ndash 1273 pmid 13827775 cite journal author GRYDER RM, POGELL BM year 1960 title Further studies on glucosamine 6 phosphate synthesis by rat liver enzymes journal J. Biol. Chem. volume 235 ... more details
OrganicBox complete wiki name Glutamine name 2S 2 amino 4 carbamoyl butanoic acid GENERAL INFORMATION C 5 H 10 N 2 O 3 mass 146.15 abbreviation Q, Gln image Image L glutamine skeletal.png 190px Chemical structure of Glutamine br Image L glutamine 3D sticks.png 205px Chemical structure of the amino acid glutamine synonyms D L Glutamine br 2 amino 4 carbamoylbutanoic acid br L D 2 aminoglutaramic acid br AI3 32686 br C00303 br Cebrogen br G107 br Glumin br Glutamic acid 5 amide br L D glutamid br Miglu P br NSC 97925 br NSC27421 DATABASES SMILES NC O CCC N C O O InChI 1 C5H10N2O3 c6 3 5 9 10 1 2 4 7 8 h3H,1 2,6H2, H2,7,8 H,9,10 f h9H,7H2 ATC prefix ATC suffix ATC supplemental CAS 56 85 9 DrugBank EINECS 200 292 1 PubChem br 738 ref 1 a , 145815 D ref 2 a , 5961 L ref 3 a PHYSICAL PROPERTIES Structure index of refraction abbe number dielectric constant magnetic susceptibility dipole moment U V data lambda max extinction coefficient Infrared data absorption bands NMR data proton NMR carbon NMR other NMR Spectrometry data mass spectrometry Phase behaviour delta fus H o delta fus S o delta vap H o delta vap S o triple point K triple point C triple point Pa criticle point K criticle point C criticle point Pa Solid properties delta f H o solid S o solid heat capacity solid density solid melting point C 185 melting point F melting point K Liquid properties delta f H o liquid S o liquid heat capacity liquid density liquid viscosity liquid boiling point C boiling point F boiling point K Gas properties delta f H o gas S o gas heat capacity gas viscosity gas HAZARD PROPERTIES MSDS main hazards nfpa health nfpa flammability nfpa reactivity nfpa special flash point r phrases s phrases RTECS number CHEMICAL PROPERTIES XLogP 4.102 isoelectric point 5.65 disociation constant 2.18 9.00 tautomers 2 H bond donor 3 H bond acceptor 4 PHARMACOLOGICAL PROPERTIES bioavailability metabolism elimination half life excretion pregnancy category legal status routes of administration References ... more details
enzyme Name protein glutamine gamma glutamyltransferase EC number 2.3.2.13 CAS number 80146 85 6 IUBMB EC number 2 3 2 13 GO code 0003810 image width caption Orphan date February 2009 In enzymology , a protein glutamine gamma glutamyltransferase EC number 2.3.2.13 is an enzyme that catalysis catalyzes the chemical reaction protein glutamine alkylamine math rightleftharpoons math protein N sub 5 sub alkylglutamine NH sub 3 sub Thus, the two substrate biochemistry substrates of this enzyme are protein glutamine and Amine Aliphatic amines alkylamine , whereas its two product chemistry products are protein N 5 alkylglutamine and ammonia NH sub 3 sub . This enzyme participates in complement system complement and coagulation cascade s and Huntington s disease . It employs one cofactor biochemistry cofactor , calcium . Nomenclature This enzyme belongs to the family of transferase s, specifically the aminoacyltransferases . The systematic name of this enzyme class is protein glutamine amine gamma glutamyltransferase . Other names in common use include div col colwidth 30em factor XIIIa, fibrin stabilizing factor, fibrinoligase, glutaminylpeptide gamma glutamyltransferase, polyamine transglutaminase, R glutaminyl peptide amine gamma glutamyl transferase tissue transglutaminase, and transglutaminase. Div col end Structural studies As of late 2007, 19 tertiary structure structures have been solved for this class of enzymes, with Protein Data Bank PDB accession codes PDB link 1EVU , PDB link 1EX0 , PDB link 1F13 , PDB link 1FIE , PDB link 1G0D , PDB link 1GGT , PDB link 1GGU , PDB link 1GGY , PDB link 1IU4 , PDB link 1KV3 , PDB link 1L9M , PDB link 1L9N , PDB link 1NUD , PDB link 1NUF , PDB link 1NUG , PDB link 1QRK , PDB link 1RLE , PDB link 1SGX , and PDB link 1VJJ . References reflist 1 refbegin cite journal author Folk JE, Chung SI date 1973 title Molecular and catalytic properties of transglutaminases journal Adv. Enzymol. Relat. Areas. Mol. Biol. volume 38 pages 109&ndash ... more details
catfish, Clarias batrachus upregulates glutaminesynthetase and carbamyl phosphate synthetase III ... phosphate synthetase by the antibiotic acivicin Pfam PF00988 Pfam clan InterPro IPR002474 SMART PROSITE PDOC00676 MEROPS SCOP 1jdb TCDB OPM family OPM protein CAZy CDD Carbamoyl phosphate synthetase catalyzes the ATP dependent synthesis of carbamoyl phosphate from glutamine EC number 6.3.5.5 or ammonia ..., Scully JL, Evans DR, Rinker Jr AG title Mammalian carbamyl phosphate synthetase CPS . DNA sequence ... author Holden HM, Thoden JB, Raushel FM title Carbamoyl phosphate synthetase an amazing biochemical ... Carbamoyl phosphate synthetase I mitochondria, urea cycle Carbamoyl phosphate synthetase II cytosol, pyrimidine metabolism . Carbamoyl phosphate synthetase III found in fish . ref name pmid17451989 ... and synthetase protein domain domains . ref name pmid17451989 ref name pmid10387030 cite ... subunit contains the glutamine binding site and biocatalysis catalyses the hydrolysis of glutamine ... has glutamine amidotransferase activity. The large subunit has two Homology biology homologous ... domain of carbamoyl phosphate synthetase journal Biochemistry volume 35 issue 45 pages 14352 61 year ..., Rayment I, Holden HM title The structure of carbamoyl phosphate synthetase determined to 2.1 A resolution ... tunnel of carbamoyl phosphate synthetase journal Biochemistry volume 41 issue 42 pages 12575 81 ... more details
Infobox Disease Name Holocarboxylase synthetase deficiency Image biotin structure.svg Caption Biotin DiseasesDB 32709 ICD10 ICD9 ICDO OMIM 253270 MedlinePlus eMedicineSubj ped eMedicineTopic 1020 MeshID D028922 br Holocarboxylase synthetase deficiency is an Biological inheritance inherited metabolic disorder in which the body is unable to use the vitamin biotin effectively. This disorder is classified as a multiple carboxylase deficiency , a group of disorders characterized by impaired activity of certain enzyme s that depend on biotin. Symptoms are very similar to biotinidase deficiency and treatment large doses of biotin is also the same. Diagnosis The signs and symptoms of holocarboxylase synthetase deficiency typically appear within the first few months of life, but the age of onset varies. Affected infants often have immunodeficiency diseases, difficulty feeding, breathing problems, a skin rash , hair loss alopecia , and a lack of energy lethargy . Immediate treatment and lifelong management using biotin supplements may prevent many of these complications. If left untreated, the disorder can lead to delayed development, seizure s, and coma . These medical problems may be life threatening in some cases. Genetics Image autorecessive.svg thumb right Holocarboxylase synthetase deficiency has an autosomal recessive pattern of inheritance. Mutation s in the HLCS gene cause holocarboxylase synthetase deficiency. The HLCS gene makes an enzyme , holocarboxylase synthetase , that attaches biotin to other molecules. Biotin, a B vitamin , is found in foods such as liver , egg yolk s, and milk . It is essential for the normal production and breakdown of protein s, lipid fat s, and carbohydrate s in the body. Mutations in the HLCS gene reduce the activity of holocarboxylase synthetase, preventing cells from using biotin effectively and disrupting many cellular functions. This condition is inherited in an autosomal recessive pattern, which means two copies of the gene in each ... more details
Refimprove date July 2008 Infobox Disease Name Glutathione synthetase deficiency Image Glutathion.svg Caption Glutathione DiseasesDB 29839 ICD10 ICD9 ICDO OMIM 266130 MedlinePlus eMedicineSubj ped eMedicineTopic 867 MeshID Glutathione synthetase deficiency is a rare autosomal recessive ref cite journal pages 384 9 doi 10.1007 s00439 005 1255 6 title Genotype, enzyme activity, glutathione level, and clinical phenotype in patients with glutathione synthetase deficiency year 2005 last1 Nj lsson first1 Runa last2 Ristoff first2 Ellinor last3 Carlsson first3 Katarina last4 Winkler first4 Andreas last5 Larsson first5 Agne last6 Norgren first6 Svante journal Human Genetics volume 116 issue 5 pmid 15717202 ref metabolic disorder that prevents the production of glutathione . Glutathione helps prevent damage to cells by neutralizing harmful molecules generated during energy production. Glutathione ... DNA , proteins, and other important cellular components. Diagnosis Glutathione synthetase deficiency ... 45 doi 10.1007 s00018 005 5163 7 title Glutathione synthetase deficiency year 2005 last1 Nj lsson ... synthetase deficiency usually results in the destruction of red blood cells hemolytic anemia ... glutathione synthetase deficiency may experience symptoms beginning shortly after birth including ... . In addition to the features present in moderate glutathione synthetase deficiency, individuals ... synthetase deficiency also develop recurrent bacterial infections. Genetics Image autorecessive.svg thumb right Glutathione synthetase deficiency has an autosomal recessive pattern of inheritance. Mutations in the GSS gene cause glutathione synthetase deficiency. This gene provides instructions for making the enzyme glutathione synthetase . This enzyme is involved in a process called the gamma ... levels of glutathione, leading to the signs and symptoms of glutathione synthetase deficiency. This disorder ... glutathione synthetase deficiency leads not only to glutathione but also to glutathione S transferase ... more details
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