Kob(I)irinska kiselina a,c-diamid adenoziltransferaza
| Kob(I)irinska kiselina a,c-diamid adenoziltransferaza | |||||||||
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| Identifikatori | |||||||||
| EC broj | 2.5.1.17 | ||||||||
| CAS broj | 37277-84-2 | ||||||||
| Baze podataka | |||||||||
| IntEnz | IntEnz pregled | ||||||||
| BRENDA | BRENDA pristup | ||||||||
| ExPASy | NiceZyme pregled | ||||||||
| KEGG | KEGG pristup | ||||||||
| MetaCyc | metabolički put | ||||||||
| PRIAM | profil | ||||||||
| Strukture PBP | RCSB PDB PDBe PDBj PDBsum | ||||||||
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Kob(I)irinska kiselina a,c-diamid adenoziltransferaza (EC 2.5.1.17, CobA, CobO, ATP:korinoidna adenoziltransferaza, kob(I)alaminska adenoziltransferaza, akvakob(I)alaminska adenoziltransferaza, akvokob(I)alamin vitamin B12s adenoziltransferaza, ATP:kob(I)alamin Cobeta-adenoziltransferaza) je enzim sa sistematskim imenom ATP:kob(I)irinska kiselina-a,c-diamid Cobeta-adenoziltransferaza.[1][2][3][4] Ovaj enzim katalizuje sledeću hemijsku reakciju
- (1) ATP + kob(I)irinska kiselina a,c-diamid trifosfat + adenozilkob(III)irinska kiselina a,c-diamid
- (2) ATP + kobinamid trifosfat + adenozilkobinamid
Korinoidna adenozilacija se odvija u tri stupnja: (i) redukcija Co(III) do Co(II) putem transvera jednog elektrona. To može da bude posredovano enzimom EC 1.16.1.3, akvakabalaminska reduktaza ili neenzimatski u prisustvu dihidroflavinskih nukleotida. (ii) Co(II) se redukuje do Co(I) u drugom transferu jednog elektrona posredstvom enzima EC 1.16.1.4, kob(II)alamin reduktaze i (iii) Co(I) izvodi nukleofilni napad na adenozilnu grupu ATP-a ostavljajući atom kobalta u Co(III) stanju (EC 2.5.1.17).
Reference
[уреди | уреди извор]- ^ Vitols, E., Walker, G.A. and Huennekens, F.M. (1966). „Enzymatic conversion of vitamin B12s to a cobamide coenzyme, α-(5,6-dimethylbenzimidazolyl)deoxyadenosylcobamide (adenosyl-B12)”. J. Biol. Chem. 241: 1455—1461. PMID 5946606.
- ^ Bauer, C.B., Fonseca, M.V., Holden, H.M., Thoden, J.B., Thompson, T.B., Escalante-Semerena, J.C. and Rayment, I. (2001). „Three-dimensional structure of ATP:corrinoid adenosyltransferase from Salmonella typhimurium in its free state, complexed with MgATP, or complexed with hydroxycobalamin and MgATP”. Biochemistry. 40: 361—374. PMID 11148030.
- ^ Fonseca, M.V. & Escalante-Semerena, J.C. (2001). „An in vitro reducing system for the enzymic conversion of cobalamin to adenosylcobalamin”. J. Biol. Chem. 276: 32101—32108. PMID 11408479.
- ^ Suh, S. & Escalante-Semerena, J.C. (1995). „Purification and initial characterization of the ATP:corrinoid adenosyltransferase encoded by the cobA gene of Salmonella typhimurium”. J. Bacteriol. 177: 921—925. PMID 7860601.
Literatura
[уреди | уреди извор]- Nicholas C. Price; Lewis Stevens (1999). Fundamentals of Enzymology: The Cell and Molecular Biology of Catalytic Proteins (Third изд.). USA: Oxford University Press. ISBN 019850229X.
- Eric J. Toone (2006). Advances in Enzymology and Related Areas of Molecular Biology, Protein Evolution (Volume 75 изд.). Wiley-Interscience. ISBN 0471205036.
- Branden C; Tooze J. Introduction to Protein Structure. New York, NY: Garland Publishing. ISBN 0-8153-2305-0.
- Irwin H. Segel. Enzyme Kinetics: Behavior and Analysis of Rapid Equilibrium and Steady-State Enzyme Systems (Book 44 изд.). Wiley Classics Library. ISBN 0471303097.
Spoljašnje veze
[уреди | уреди извор]- Cob(I)yrinic+acid+a,c-diamide+adenosyltransferase на US National Library of Medicine Medical Subject Headings (MeSH)
