KEGG   ENZYME: 1.14.11.28
Entry
EC 1.14.11.28               Enzyme                                 
Name
proline 3-hydroxylase;
P-3-H
Class
Oxidoreductases;
Acting on paired donors, with incorporation or reduction of molecular oxygen;
With 2-oxoglutarate as one donor, and incorporation of one atom of oxygen into each donor
Sysname
L-proline,2-oxoglutarate:oxygen oxidoreductase (3-hydroxylating)
Reaction(IUBMB)
L-proline + 2-oxoglutarate + O2 = cis-3-hydroxy-L-proline + succinate + CO2 [RN:R09572]
Reaction(KEGG)
R09572
Substrate
L-proline [CPD:C00148];
2-oxoglutarate [CPD:C00026];
O2 [CPD:C00007]
Product
cis-3-hydroxy-L-proline [CPD:C19706];
succinate [CPD:C00042];
CO2 [CPD:C00011]
Comment
Requires iron(II) for activity. Unlike the proline hydroxylases involved in collagen biosynthesis [EC 1.14.11.2 (procollagen-proline dioxygenase) and EC 1.14.11.7 (procollagen-proline 3-dioxygenase)], this enzyme does not require ascorbate for activity although it does increase the activity of the enzyme [2]. The enzyme is specific for L-proline as D-proline, trans-4-hydroxy-L-proline, cis-4-hydroxy-L-proline and 3,4-dehydro-DL-proline are not substrates [2].
History
EC 1.14.11.28 created 2006
Orthology
K20149  proline 3-hydroxylase
Reference
1  [PMID:16535329]
  Authors
Mori H, Shibasaki T, Uozaki Y, Ochiai K, Ozaki A.
  Title
Detection of Novel Proline 3-Hydroxylase Activities in Streptomyces and Bacillus spp. by Regio- and Stereospecific Hydroxylation of l-Proline.
  Journal
Appl Environ Microbiol 62:1903-1907 (1996)
DOI:10.1128/AEM.62.6.1903-1907.1996
Reference
2  [PMID:9294421]
  Authors
Mori H, Shibasaki T, Yano K, Ozaki A
  Title
Purification and cloning of a proline 3-hydroxylase, a novel enzyme which hydroxylates free L-proline to cis-3-hydroxy-L-proline.
  Journal
J Bacteriol 179:5677-83 (1997)
DOI:10.1128/JB.179.18.5677-5683.1997
  Sequence
[ag:BAA22406]
Reference
3  [PMID:11737217]
  Authors
Clifton IJ, Hsueh LC, Baldwin JE, Harlos K, Schofield CJ
  Title
Structure of proline 3-hydroxylase. Evolution of the family of 2-oxoglutarate dependent oxygenases.
  Journal
Eur J Biochem 268:6625-36 (2001)
DOI:10.1046/j.0014-2956.2001.02617.x
Other DBs
ExplorEnz - The Enzyme Database: 1.14.11.28
IUBMB Enzyme Nomenclature: 1.14.11.28
ExPASy - ENZYME nomenclature database: 1.14.11.28
BRENDA, the Enzyme Database: 1.14.11.28
CAS: 162995-24-6

  All links  
Chemical substance (6)   
   KEGG COMPOUND (6)   
Chemical reaction (2)   
   KEGG REACTION (1)   
   KEGG RCLASS (1)   
Gene (2)   
   KEGG ORTHOLOGY (1)   
   KEGG GENES (1)   
Protein sequence (11)   
   UniProt (9)   
   SWISS-PROT (2)   
DNA sequence (6)   
   GenBank (3)   
   EMBL (3)   
Protein domain (4)   
   InterPro (4)   
All databases (31)   

Download RDF
DBGET integrated database retrieval system