KEGG   ENZYME: 1.11.1.20Help
Entry
EC 1.11.1.20                Enzyme                                 

Name
prostamide/prostaglandin F2alpha synthase;
prostamide/PGF synthase;
prostamide F synthase;
prostamide/prostaglandin F synthase;
tPGF synthase
Class
Oxidoreductases;
Acting on a peroxide as acceptor;
Peroxidases
BRITE hierarchy
Sysname
thioredoxin:(5Z,9alpha,11alpha,13E,15S)-9,11-epidioxy-15-hydroxy-prosta-5,13-dienoate oxidoreductase
Reaction(IUBMB)
thioredoxin + (5Z,9alpha,11alpha,13E,15S)-9,11-epidioxy-15-hydroxy-prosta-5,13-dienoate = thioredoxin disulfide + (5Z,9alpha,11alpha,13E,15S)-9,11,15-trihydroxyprosta-5,13-dienoate [RN:R09506]
Reaction(KEGG)
Substrate
thioredoxin [CPD:C00342];
(5Z,9alpha,11alpha,13E,15S)-9,11-epidioxy-15-hydroxy-prosta-5,13-dienoate [CPD:C00427]
Product
thioredoxin disulfide [CPD:C00343];
(5Z,9alpha,11alpha,13E,15S)-9,11,15-trihydroxyprosta-5,13-dienoate [CPD:C00639]
Comment
The enzyme contains a thioredoxin-type disulfide as a catalytic group. Prostamide H2 and prostaglandin H2 are the best substrates; the latter is converted to prostaglandin F2alpha. The enzyme also reduces tert-butyl hydroperoxide, cumene hydroperoxide and H2O2, but not prostaglandin D2 or prostaglandin E2.
History
EC 1.11.1.20 created 2011
Pathway
ec00590  Arachidonic acid metabolism
ec01100  Metabolic pathways
Orthology
K15717  prostamide/prostaglandin F2alpha synthase
Genes
HSA: 127281(PRXL2B)
PTR: 744202(FAM213B)
PPS: 100989393(FAM213B)
GGO: 101134253(FAM213B)
PON: 100190803(FAM213B)
NLE: 100586906(FAM213B)
MCC: 695160(FAM213B)
MCF: 102136927(FAM213B)
CSAB: 103225752(FAM213B)
RRO: 104664581(FAM213B)
RBB: 108526093 108536020(FAM213B)
CJC: 100403434(FAM213B)
SBQ: 101029200(FAM213B)
MMU: 66469(Fam213b)
RNO: 362676(Fam213b)
CGE: 100755514(Fam213b)
NGI: 103749778(Fam213b)
HGL: 101722975(Fam213b)
CCAN: 109691456(Fam213b)
TUP: 102487629(FAM213B)
CFA: 489616(FAM213B)
AML: 100476330(FAM213B)
UMR: 103678433(FAM213B)
ORO: 101379247(FAM213B)
FCA: 101090122(FAM213B)
PTG: 102951174(FAM213B)
AJU: 106984648(FAM213B)
BTA: 617001(FAM213B)
BOM: 102268856(FAM213B)
BIU: 109570724(FAM213B)
PHD: 102339391
CHX: 102184926(FAM213B)
OAS: 101120767(FAM213B)
SSC: 100134955(FAM213B)
CFR: 102509927(FAM213B)
CDK: 105106649(FAM213B)
BACU: 103000861(FAM213B)
LVE: 103071802(FAM213B)
OOR: 101284921(FAM213B)
ECB: 100054405(FAM213B)
EPZ: 103545047(FAM213B)
EAI: 106844791(FAM213B)
HAI: 109391141(FAM213B)
RSS: 109461136(FAM213B)
PALE: 102887804(FAM213B)
LAV: 100674527(FAM213B)
TMU: 101348540
MDO: 100027973(FAM213B)
SHR: 100932106(FAM213B)
ASN: 102371358(FAM213B)
AMJ: 102569997(FAM213B)
PSS: 102455880(FAM213B)
CMY: 102948080(FAM213B)
CPIC: 101934510(FAM213B)
PVT: 110088238(FAM213B)
GJA: 107110400(FAM213B)
XLA: 447017(fam213b.L)
XTR: 549974(fam213b)
NPR: 108783702(FAM213B)
DRE: 406605(prxl2b)
CCAR: 109098633
IPU: 108254989(fam213b)
AMEX: 103027709(fam213b)
TRU: 101064795(fam213b)
LCO: 104919355(fam213b)
NCC: 104955273(fam213b)
MZE: 101467269(fam213b)
OLA: 101173382(fam213b)
XMA: 102226891(fam213b)
PRET: 103464468(fam213b)
NFU: 107385267(fam213b)
CSEM: 103385682(fam213b)
LCF: 108899895(fam213b)
HCQ: 109529232(fam213b)
BPEC: 110166956(fam213b)
SASA: 106582827(fam213b)
ELS: 105017396(fam213b)
SFM: 108918216(fam213b)
LCM: 102361632(FAM213B)
CIN: 100184332
SPU: 591310
APLC: 110985701
BMOR: 101742192
PMAC: 106709420
PRAP: 111000037
FCD: 110852137
CRG: 105330608
MYI: 110460228
EGL: EGR_01663
EPA: 110247772
ADF: 107339164
HMG: 100198146
AAF: AURANDRAFT_77989(SelU1)
 » show all
Taxonomy
Reference
1  [PMID:18006499]
  Authors
Moriuchi H, Koda N, Okuda-Ashitaka E, Daiyasu H, Ogasawara K, Toh H, Ito S, Woodward DF, Watanabe K
  Title
Molecular characterization of a novel type of prostamide/prostaglandin F synthase, belonging to the thioredoxin-like superfamily.
  Journal
J Biol Chem 283:792-801 (2008)
DOI:10.1074/jbc.M705638200
  Sequence
[ssc:100134955]
Reference
2  [PMID:20950588]
  Authors
Yoshikawa K, Takei S, Hasegawa-Ishii S, Chiba Y, Furukawa A, Kawamura N, Hosokawa M, Woodward DF, Watanabe K, Shimada A
  Title
Preferential localization of prostamide/prostaglandin F synthase in myelin sheaths of the central nervous system.
  Journal
Brain Res 1367:22-32 (2011)
DOI:10.1016/j.brainres.2010.10.019
  Sequence
[mmu:66469]
Other DBs
ExplorEnz - The Enzyme Database: 1.11.1.20
IUBMB Enzyme Nomenclature: 1.11.1.20
ExPASy - ENZYME nomenclature database: 1.11.1.20
BRENDA, the Enzyme Database: 1.11.1.20

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