EC number:1.14.11.2

Enzyme

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     1. Oxidoreductases
        1.14 Acting on paired donors, with incorporation or reduction of molecular oxygen
            1.14.11 With 2-oxoglutarate as one donor, and incorporation of one atom of oxygen into each donor
ID:1.14.11.2
Description:Procollagen-proline 4-dioxygenase.
Alternative Name: Protocollagen hydroxylase.
Prolyl hydroxylase.
Prolyl 4-hydroxylase.
Proline,2-oxoglutarate 4-dioxygenase.
Proline hydroxylase.
Procollagen-proline,2-oxoglutarate-4-dioxygenase.
Procollagen-proline dioxygenase.
Prosite: PDOC51471; PDOC00172;
PDB:
PDBScop
4NHM 8045291; 8089987; 8089988; 8089989;
4NHL 8045291; 8089987; 8089988; 8089989;
4NHK 8045291; 8089987; 8089988; 8089989;
3MGU 8045291; 8089987; 8089988; 8089989;
3KT7 8045291; 8089987; 8089988; 8089989;
 » show all
Cath: 1.10.1720.10; 1.10.287.3220; 1.25.40.10; 2.60.120.330;

3D structure

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PDB

References

External Links

UniProtKB Enzyme Link: UniProtKB 1.14.11.2
BRENDA Enzyme Link: BRENDA 1.14.11.2
KEGG Enzyme Link: KEGG1.14.11.2
BioCyc Enzyme Link: BioCyc 1.14.11.2
ExPASy Enzyme Link: ExPASy1.14.11.2
EC2PDB Enzyme Link: EC2PDB 1.14.11.2
ExplorEnz Enzyme Link: ExplorEnz 1.14.11.2
PRIAM enzyme-specific profiles Link: PRIAM 1.14.11.2
IntEnz Enzyme Link: IntEnz 1.14.11.2
MEDLINE Enzyme Link: MEDLINE 1.14.11.2

EC number:1.14.11.2

MSA:

1.14.11.2;
Phylogenetic Tree:

1.14.11.2;
Uniprot:
M-CSA:
RHEA:18945 2-oxoglutarate + L-prolyl-[procollagen] + O2 = CO2 + succinate + trans-4-hydroxy-L-prolyl-[procollagen]
RULE(radius=1) [*:1]-[CH2;+0:2]-[*:3].[*:4]=[C;H0;+0:5](-[OH;+0:6])-[C;H0;+0:7](=[*:8])-[*:9].[O;H0;+0:10]=[O;H0;+0:11]>>[*:1]-[CH;+0:2](-[*:3])-[OH;+0:10].[*:8]=[C;H0;+0:7](-[*:9])-[OH;+0:11].[*:4]=[C;H0;+0:5]=[O;H0;+0:6]
Reaction
Core-to-Core No scaffolds atoms were exchanged as a result of the reaction

References

TitleAuthorsDatePubMed ID
Mechanism of the prolyl hydroxylase reaction. 2. Kinetic analysis of the reaction sequence.Myllylä R, Tuderman L, Kivirikko KI1977 Nov 1200425
Mechanism of the prolyl hydroxylase reaction. 1. Role of co-substrates.Tuderman L, Myllylä R, Kivirikko KI1977 Nov 1200424
Stringency of the 2-His-1-Asp active-site motif in prolyl 4-hydroxylase.Gorres KL, Pua KH, Raines RT2009 Nov 519890397
Structural basis for binding of hypoxia-inducible factor to the oxygen-sensing prolyl hydroxylases.Chowdhury R, McDonough MA, Mecinović J, Loenarz C, Flashman E, Hewitson KS, Domene C, Schofield CJ2009 Jul 1519604478
The crystal structure of an algal prolyl 4-hydroxylase complexed with a proline-rich peptide reveals a novel buried tripeptide binding motif.Koski MK, Hieta R, Hirsilä M, Rönkä A, Myllyharju J, Wierenga RK2009 Sep 1119553701
Prolyl 4-hydroxylases, key enzymes in the synthesis of collagens and regulation of the response to hypoxia, and their roles as treatment targets.Myllyharju J200819160570
The kinetics of the hydroxylation of procollagen by prolyl 4-hydroxylase. Proposal for a processive mechanism of binding of the dimeric hydroxylating enzyme in relation to the high kcat/Km ratio and a conformational requirement for hydroxylation of -X-Pro-Gly- sequences.de Jong L, van der Kraan I, de Waal A1991 Aug 91653613
Characterization of a second Arabidopsis thaliana prolyl 4-hydroxylase with distinct substrate specificity.Tiainen P, Myllyharju J, Koivunen P2005 Jan 1415528200
Cloning and characterization of a low molecular weight prolyl 4-hydroxylase from Arabidopsis thaliana. Effective hydroxylation of proline-rich, collagen-like, and hypoxia-inducible transcription factor alpha-like peptides.Hieta R, Myllyharju J2002 Jun 2811976332