PBB geneid 3032 Trifunctional enzyme subunit beta, mitochondrial TP beta also known as 3 ketoacyl CoA thiolase , acetyl CoA acyltransferase , or beta ketothiolase is an enzyme that in humans is encoded by the HADHB gene . ref name entrez cite web title Entrez Gene hydroxyacyl Coenzyme A dehydrogenase 3 ketoacyl Coenzyme A thiolase enoyl Coenzyme A hydratase trifunctional protein url http www.ncbi.nlm.nih.gov sites entrez?Db gene&Cmd ShowDetailView&TermToSearch 3032 accessdate ref HADHB is a subunit of the mitochondrial trifunctional protein and has thiolase activity. Function This gene encodes the beta subunit of the mitochondrial trifunctional protein, which catalyzes the last three steps of mitochondrial beta oxidation of long chain fatty acids. The mitochondrial membrane bound heterocomplex is composed of four alpha and four beta subunits, with the beta subunit catalyzing the 3 ketoacyl CoA thiolase activity. Mutations in this gene result in trifunctional protein deficiency. The encoded protein can also bind RNA and decreases the stability of some mRNAs. The genes of the alpha and beta subunits of the mitochondrial trifunctional protein are located adjacent to each other in the human genome in a head to head orientation. ref name entrez References reflist Further reading refbegin 2 cite journal author Wang R, Yang Z, Zhu JM, et al. title Screening for G1528C mutation in mitochondrial trifunctional protein gene in pregnant women with severe preeclampsia and new born infant . journal Zhonghua Fu Chan Ke Za Zhi volume 41 issue 10 pages 672 5 year 2006 pmid 17199921 doi cite journal author Aboulaich N, Vainonen JP, Str lfors P, Vener AV title Vectorial proteomics reveal targeting, phosphorylation and specific fragmentation of polymerase I and transcript release factor PTRF at the surface of caveolae in human adipocytes. journal Biochem. J. volume 383 issue Pt 2 pages 237 48 year 2004 pmid 15242332 doi 10.1042 BJ20040647 pmc 1134064 cite journal author Adams DJ, Beve ... more details
http www.pdb.org pdb static.do?p education discussion molecule of the month pdb26 1.html more details... enzyme Name nitrogenase EC number 1.18.6.1 CAS number 9013 04 1 IUBMB EC number 1 18 6 1 GO code image width caption Nitrogenases EC number 1.18.6.1 EC number 1.19.6.1 are enzyme s used by some organisms to fix atmospheric nitrogen gas N sub 2 sub . It is the only known family of enzymes that accomplish this process. Dinitrogen is quite inert because of the strength of its N N triple bond . To break one nitrogen atom away from another requires breaking all three of these chemical bonds. Whilst the equilibrium formation of ammonia from molecular hydrogen and nitrogen has an overall negative enthalpy of reaction H sup 0 sup 45.2 kJ mol sup 1 sup NH sub 3 sub , the Activation energy energy barrier to activation is very high E sub A sub 420 kJ mol sup 1 sup without the assistance of catalysis. ref Modak, J. M., 2002, Haber Process for Ammonia Synthesis, Resonance . 7, 69 77. ref In addition to reducing agents , such as dithionite in vitro , or ferredoxin or flavodoxin in vivo , the enzymatic reduction of dinitrogen to ammonia therefore also requires an input of chemical energy, released from the hydrolysis of Adenosine triphosphate ATP , to overcome the activation energy barrier. The enzyme is composed of the heterotetrameric MoFe protein that is transiently associated with the homodimeric Fe protein . Electrons for the reduction of nitrogen are supplied to nitrogenase when it associates with the reduced, nucleotide bound homodimeric Fe protein. The heterocomplex undergoes cycles of cycle of association association and disassociation to transfer one electron , which is the rate limiting step in nitrogen reduction. ATP supplies the energy to drive the transfer of electrons from the Fe protein to the MoFe protein. The reduction potential of each electron transferred to the MoFe protein is sufficient to break one of dinitrogen s chemical bonds, though it has not yet be ... more details
PBB geneid 7133 Tumor necrosis factor receptor superfamily member 1B is a protein that in humans is encoded by the TNFRSF1B gene . ref name pmid2158863 cite journal author Schall TJ, Lewis M, Koller KJ, Lee A, Rice GC, Wong GH, Gatanaga T, Granger GA, Lentz R, Raab H, et al. title Molecular cloning and expression of a receptor for human tumor necrosis factor journal Cell volume 61 issue 2 pages 361 70 year 1990 month Jun pmid 2158863 pmc doi 10.1016 0092 8674 90 90816 W ref ref name pmid8702885 cite journal author Santee SM, Owen Schaub LB title Human tumor necrosis factor receptor p75 80 CD120b gene structure and promoter characterization journal J Biol Chem volume 271 issue 35 pages 21151 9 year 1996 month Oct pmid 8702885 pmc doi 10.1074 jbc.271.35.21151 ref The protein encoded by this gene is a member of the Tumor necrosis factor receptor superfamily, which also contains TNFRSF1A. The protein encoded by this gene is a member of the TNF receptor superfamily. This protein and TNF receptor 1 form a heterocomplex that mediates the recruitment of two anti apoptotic proteins, c IAP1 and c IAP2, which possess E3 ubiquitin ligase activity. The function of IAPs in TNF receptor signalling is unknown, however, c IAP1 is thought to potentiate TNF induced apoptosis by the ubiquitination and degradation of TNF receptor associated factor 2, which mediates anti apoptotic signals. Knockout studies in mice also suggest a role of this protein in protecting neurons from apoptosis by stimulating antioxidative pathways. ref cite web title Entrez Gene TNFRSF1B tumor necrosis factor receptor superfamily, member 1B url http www.ncbi.nlm.nih.gov sites entrez?Db gene&Cmd ShowDetailView&TermToSearch 7133 accessdate ref Interactions TNFRSF1B has been shown to Protein protein interaction interact with TTRAP ref name pmid10764746 cite journal last Pype first S authorlink coauthors Declercq W, Ibrahimi A, Michiels C, Van Rietschoten J G, Dewulf N, de Boer M, Vandenabeele P, Huylebroeck D, Rema ... more details
heterocomplex assembly journal J. Biol. Chem. volume 277 issue 37 pages 33698 703 publisher ... H, Hutchison K A, Perdew G H, Jove R, Pratt W B year 1993 month Oct. title Raf exists in a native heterocomplex ... more details
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