KEGG   ENZYME: 1.14.11.28Help
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
BRITE hierarchy
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)
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
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 (1996) 1903-1907.
  Organism
Bacillus sp., Streptomyces sp.
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 (1997) 5677-83.
  Organism
Streptomyces sp.
  Sequence
[up:P96010]
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 (2001) 6625-36.
  Organism
Streptomyces sp.
  Sequence
[up:O09345]
Other DBs
ExplorEnz - The Enzyme Database: 
IUBMB Enzyme Nomenclature: 
ExPASy - ENZYME nomenclature database: 
BRENDA, the Enzyme Database: 
CAS: 
162995-24-6

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