EC 1.14.11.4 - Procollagen-lysine 5-dioxygenase

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IntEnz Enzyme Nomenclature
EC 1.14.11.4

Names

Accepted name:
procollagen-lysine 5-dioxygenase
Other names:
collagen lysine hydroxylase
lysine hydroxylase
lysine,2-oxoglutarate 5-dioxygenase
lysine-2-oxoglutarate dioxygenase
lysyl hydroxylase
lysylprotocollagen dioxygenase
peptidyl-lysine, 2-oxoglutarate: oxygen oxidoreductase
peptidyllysine, 2-oxoglutarate:oxygen 5-oxidoreductase
protocollagen lysine dioxygenase
protocollagen lysine hydroxylase
protocollagen lysyl hydroxylase
procollagen-lysine,2-oxoglutarate 5-dioxygenase
procollagen-L-lysine,2-oxoglutarate:oxygen oxidoreductase (5-hydroxylating)
Systematic name:
L-lysine-[procollagen],2-oxoglutarate:oxygen oxidoreductase (5-hydroxylating)

Reaction

Cofactors

Comments:

Requires Fe2+ and ascorbate.

Links to other databases

Enzymes and pathways: NC-IUBMB , BRENDA , ExplorEnz , ENZYME@ExPASy , KEGG , MetaCyc , UniPathway
Protein domains and families: PROSITE:PDOC01028 , PROSITE:PDOC51471
Structural data: CSA , EC2PDB
Gene Ontology: GO:0008475
CAS Registry Number: 9059-25-0
UniProtKB/Swiss-Prot: (16) [show] [UniProt]

References

  1. Hausmann, E.
    Cofactor requirements for the enzymatic hydroxylation of lysine in a polypeptide precursor of collagen.
    Biochim. Biophys. Acta 133: 591-598 (1967). [PMID: 6033801]
  2. Rhoads, R.E. and Udenfriend, S.
    Decarboxylation of α-ketoglutarate coupled to collagen proline hydroxylase.
    Proc. Natl. Acad. Sci. USA 60: 1473-1478 (1968). [PMID: 5244754]
  3. Puistola, U., Turpeenniemi-Hujanen, T. M., Myllyla, R., Kivirikko, K. I.
    Studies on the lysyl hydroxylase reaction. I. Initial velocity kinetics and related aspects.
    Biochim. Biophys. Acta 611: 40-50 (1980). [PMID: 6766066]
  4. Puistola, U., Turpeenniemi-Hujanen, T. M., Myllyla, R., Kivirikko, K. I.
    Studies on the lysyl hydroxylase reaction. II. Inhibition kinetics and the reaction mechanism.
    Biochim. Biophys. Acta 611: 51-60 (1980). [PMID: 6766067]

[EC 1.14.11.4 created 1972, modified 1983]