Sequence of CBR1_PIG
EC Number:1.1.1.189
EC Number
Recommended Name
Accession Code
Organism
No of amino acids
Molecular Weight [Da]
Source
Reaction
(5Z,13E)-(15S)-9alpha,11alpha,15-trihydroxyprosta-5,13-dienoate + NADP+ = (5Z,13E)-(15S)-11alpha,15-dihydroxy-9-oxoprosta-5,13-dienoate + NADPH + H+
Other sequences found for EC No. 1.1.1.189
General information:
Sequence
0 MSSNTRVALV TGANKGIGFA IVRDLCRQFA GDVVLTARDV ARGQAAVKQL QAEGLSPRFH
60 QLDIIDLQSI RALCDFLRKE YGGLDVLVNN AAIAFQLDNP TPFHIQAELT MKTNFMGTRN
120 VCTELLPLIK PQGRVVNVSS TEGVRALNEC SPELQQKFKS ETITEEELVG LMNKFVEDTK
180 NGVHRKEGWS DSTYGVTKIG VSVLSRIYAR KLREQRAGDK ILLNACCPGW VRTDMGGPKA
240 PKSPEVGAET PVYLALLPSD AEGPHGQFVT DKKVVEWGVP PESYPWVNA
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Sequence Reference
Authors
Title
Journal
Volume
Pages
Year
PubMed ID
273559
Tanaka M.,Ohno S.,Nakajin S.,Shinoda M.,Nagahama Y.
Pig testicular 20-beta-hydroxysteroid dehydrogenase exhibits carbonyl reductase-like structure and activity: cDNA cloning of pig testicular 2-beta-hydroxysteroid dehydrogenase.
J. Biol. Chem.
267
13451-13455
1992
273560
Schieber A.,Frank R.W.,Ghisla S.
Purification and properties of prostaglandin 9-ketoreductase from pig and human kidney. Identity with human carbonyl reductase.
Eur. J. Biochem.
206
491-502
1992
273561
Ghosh D.,Sawicki M.,Pletnev V.,Erman M.,Ohno S.,Nakajin S.,Duax W.L.
Porcine carbonyl reductase. Structural basis for a functional monomer in short chain dehydrogenases/reductases.
J. Biol. Chem.
276
18457-18463
2001
