Holat-KoA ligaza
| Holat-KoA ligaza | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifikatori | |||||||||
| EC broj | 6.2.1.7 | ||||||||
| CAS broj | 9027-90-1 | ||||||||
| 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 | ||||||||
| |||||||||
Holat-KoA ligaza (EC 6.2.1.7, BAL, žučno kiselinska KoA ligaza, žučno kiselinska koenzim A ligaza, holoil-KoA sintetaza, holoil koenzim A sintetaza, holinska tiokinaza, holatna tiokinaza, holinska kiselina:KoA ligaza, 3alfa,7alfa,12alfa-trihidroksi-5beta-holestanoil koenzim A sintetaza, 3alfa,7alfa,12alfa-trihidroksi-5beta-holestanoat-KoA ligaza, 3alfa,7alfa,12alfa-trihidroksi-5beta-holestanoat-KoA sintetaza, THCA-KoA ligaza, 3alfa,7alfa,12alfa-trihidroksi-5beta-holestanat-KoA ligaza, 3alfa,7alfa,12alfa-trihidroksi-5beta-holestanat:KoA ligaza (formira AMP), holil-KoA sintetaza, trihidroksikoprostanoil-KoA sintetaza) je enzim sa sistematskim imenom holat:KoA ligaza (formira AMP).[1][2][3][4][5][6][7] Ovaj enzim katalizuje sledeću hemijsku reakciju
- (1) ATP + holat + KoA AMP + difosfat + holoil-KoA
- (2) ATP + (25R)-3alfa,7alfa,12alfa-trihidroksi-5beta-holestan-26-oat + KoA AMP + difosfat + (25R)-3alfa,7alfa,12alfa-trihidroksi-5beta-holestanoil-KoA
Za dejstvo ovog enzima je neophodan jon Mg2+.
Reference
[уреди | уреди извор]- ^ Elliott, W.H. (1956). „The enzymic activation of cholic acid by guinea-pig-liver microsomes”. Biochem. J. 62: 427—433. PMID 13303991.
- ^ Elliott, W.H. (1957). „The breakdown of adenosine triphosphate accompanying cholic acid activation by guinea-pig liver microsomes”. Biochem. J. 65: 315—321. PMID 13403911.
- ^ Prydz, K., Kase, B.F., Björkhem, I. and Pedersen, J.I. (1988). „Subcellular localization of 3α,7α-dihydroxy- and 3α,7α,12α-trihydroxy-5β-cholestanoyl-coenzyme A ligase(s) in rat liver”. J. Lipid Res. 29: 997—1004. PMID 3183523.
- ^ Schepers, L., Casteels, M., Verheyden, K., Parmentier, G., Asselberghs, S., Eyssen, H.J. and Mannaerts, G.P. (1989). „Subcellular distribution and characteristics of trihydroxycoprostanoyl-CoA synthetase in rat liver”. Biochem. J. 257: 221—229. PMID 2521999.
- ^ Mallonee, D.H., Adams, J.L. and Hylemon, P.B. (1992). „The bile acid-inducible baiB gene from Eubacterium sp. strain VPI 12708 encodes a bile acid-coenzyme A ligase”. J. Bacteriol. 174: 2065—2071. PMID 1551828.
- ^ Wheeler, J.B., Shaw, D.R. and Barnes, S. (1997). „Purification and characterization of a rat liver bile acid coenzyme A ligase from rat liver microsomes”. Arch. Biochem. Biophys. 348: 15—24. PMID 9390170.
- ^ Falany, C.N., Xie, X., Wheeler, J.B., Wang, J., Smith, M., He, D. and Barnes, S. (2002). „Molecular cloning and expression of rat liver bile acid CoA ligase”. J. Lipid Res. 43: 2062—2071. PMID 12454267.
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.
- William P. Jencks (1987). Catalysis in Chemistry and Enzymology. Dover Publications. ISBN 0486654605.
Spoljašnje veze
[уреди | уреди извор]- Cholate---CoA+ligase на US National Library of Medicine Medical Subject Headings (MeSH)
