The Enzyme Database

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EC 1.14.11.4     
Accepted name: procollagen-lysine 5-dioxygenase
Reaction: [procollagen]-L-lysine + 2-oxoglutarate + O2 = [procollagen]-(2S,5R)-5-hydroxy-L-lysine + succinate + CO2
Other name(s): lysine hydroxylase; lysine,2-oxoglutarate 5-dioxygenase; protocollagen lysine dioxygenase; collagen lysine hydroxylase; lysine-2-oxoglutarate dioxygenase; lysyl hydroxylase; lysylprotocollagen dioxygenase; protocollagen lysyl hydroxylase; peptidyl-lysine, 2-oxoglutarate: oxygen oxidoreductase; peptidyllysine, 2-oxoglutarate:oxygen 5-oxidoreductase; protocollagen lysine hydroxylase; procollagen-L-lysine,2-oxoglutarate:oxygen oxidoreductase (5-hydroxylating); L-lysine-[procollagen],2-oxoglutarate:oxygen oxidoreductase (5-hydroxylating)
Systematic name: [procollagen]-L-lysine,2-oxoglutarate:oxygen oxidoreductase (5-hydroxylating)
Comments: Requires Fe2+ and ascorbate.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 9059-25-0
References:
1.  Hausmann, E. Cofactor requirements for the enzymatic hydroxylation of lysine in a polypeptide precursor of collagen. Biochim. Biophys. Acta 133 (1967) 591–598. [PMID: 6033801]
2.  Rhoads, R.E. and Udenfriend, S. Decarboxylation of α-ketoglutarate coupled to collagen proline hydroxylase. Proc. Natl. Acad. Sci. USA 60 (1968) 1473–1478. [PMID: 5244754]
3.  Puistola, U., Turpeenniemi-Hujanen, T.M., Myllyla, R. and Kivirikko, K.I. Studies on the lysyl hydroxylase reaction. I. Initial velocity kinetics and related aspects. Biochim. Biophys. Acta 611 (1980) 40–50. [PMID: 6766066]
4.  Puistola, U., Turpeenniemi-Hujanen, T.M., Myllyla, R. and Kivirikko, K.I. Studies on the lysyl hydroxylase reaction. II. Inhibition kinetics and the reaction mechanism. Biochim. Biophys. Acta 611 (1980) 51–60. [PMID: 6766067]
[EC 1.14.11.4 created 1972, modified 1983]
 
 


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