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Literature summary for 1.1.1.184 extracted from

  • Imamura, Y.; Koga, T.; Shimada, H.; Otagiri, M.
    Inactivation of rabbit liver carbonyl reductase by phenylglyoxal and 2,3,4-trinitrobenzenesulfonate sodium (2003), J. Enzyme Inhib. Med. Chem., 18, 35-39.
    View publication on PubMed

Inhibitors

Inhibitors Comment Organism Structure
2,3,4-trinitrobenzenesulfonate sodium acts on a catalytic lysine located at the cofactor binding site, rapid inactivation of the liver enzyme, kinetics, NADP+, 2'-AMP, 2',5'-ADP, and 2'-phospho-5'-ADP-ribose partly protect, but 4-acetylpyridine, 5'-AMP, 5'-ADP, NMN and NAD+ do not Oryctolagus cuniculus
additional information protective effects of cofactor derivatives against inactivation by phenylglyoxal and 2,3,4-trinitrobenzenesulfonate sodium, overview Oryctolagus cuniculus
Phenylglyoxal acts on a catalytic arginine located at the cofactor binding site, rapid inactivation of the liver enzyme, kinetics, NADP+, 2'-AMP, 2',5'-ADP, and 2'-phospho-5'-ADP-ribose partly protect, but 4-acetylpyridine, 5'-AMP, 5'-ADP, NMN and NAD+ do not Oryctolagus cuniculus

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.52
-
loxoprofen pH 6.5, 30°C Oryctolagus cuniculus
0.92
-
acetohexamide pH 6.5, 30°C Oryctolagus cuniculus
1.44
-
befunolol pH 6.5, 30°C Oryctolagus cuniculus
3
-
daunorubicin pH 6.5, 30°C Oryctolagus cuniculus

Localization

Localization Comment Organism GeneOntology No. Textmining
cytosol
-
Oryctolagus cuniculus 5829
-

Organism

Organism UniProt Comment Textmining
Oryctolagus cuniculus
-
-
-

Reaction

Reaction Comment Organism Reaction ID
R-CHOH-R' + NADP+ = R-CO-R' + NADPH + H+ ordered bi bi mechanism, in which NADPH binds first and NADP+ leaves last Oryctolagus cuniculus

Source Tissue

Source Tissue Comment Organism Textmining
kidney
-
Oryctolagus cuniculus
-
liver
-
Oryctolagus cuniculus
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4-acetylpyridine + NADPH
-
Oryctolagus cuniculus ?
-
?
acetohexamide + NADPH
-
Oryctolagus cuniculus ?
-
?
befunolol + NADPH
-
Oryctolagus cuniculus ?
-
?
daunorubicin + NADPH
-
Oryctolagus cuniculus ?
-
?
loxoprofen + NADPH
-
Oryctolagus cuniculus ?
-
?
additional information substrate specificity Oryctolagus cuniculus ?
-
?

Synonyms

Synonyms Comment Organism
carbonyl reductase
-
Oryctolagus cuniculus
CR
-
Oryctolagus cuniculus
RLCR
-
Oryctolagus cuniculus

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
30
-
assay at Oryctolagus cuniculus

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
6.5
-
assay at Oryctolagus cuniculus

Cofactor

Cofactor Comment Organism Structure
NADPH catalytically important arginine and lysine residues are located in the enzymes' cofactor binding site and interact with the 2'-phosphate group of the cofactor Oryctolagus cuniculus