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Literature summary for 1.1.1.159 extracted from

  • Tanabe, T.; Tanaka, N.; Uchikawa, K.; Kabashima, T.; Ito, K.; Nonaka, T.; Mitsui, Y.; Tsuru, M.; Yoshimoto, T.
    Roles of the Ser146, Tyr159, and Lys163 residues in the catalytic action of 7alpha-hydroxysteroid dehydrogenase from Escherichia coli (1998), J. Biochem., 124, 634-641.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
site directed mutagenesis Escherichia coli

Crystallization (Commentary)

Crystallization (Comment) Organism
-
Escherichia coli

Protein Variants

Protein Variants Comment Organism
K163I 5.25% activity of wild-type activity Escherichia coli
K163R 63.7% activity of wild-type activity Escherichia coli
S146A 20.3% activity of wild-type activity Escherichia coli
S146H 35.6% activity of wild-type activity Escherichia coli
Y159F no activity Escherichia coli
Y159H 13.3% activity of wild-type activity Escherichia coli

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.159
-
NAD+ mutant K163R Escherichia coli
0.223
-
cholic acid mutant K163I Escherichia coli
0.279
-
NAD+
-
Escherichia coli
0.283
-
cholic acid mutant S146H Escherichia coli
0.302
-
NAD+ mutant S146A Escherichia coli
0.329
-
NAD+ mutant K163I Escherichia coli
0.361
-
cholic acid
-
Escherichia coli
0.364
-
NAD+ mutant S146H Escherichia coli
0.386
-
NAD+ mutant Y159H Escherichia coli
0.407
-
cholic acid mutant Y159H Escherichia coli
0.415
-
cholic acid mutant S146A Escherichia coli
0.612
-
cholic acid mutant K163R Escherichia coli

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
28000
-
4 * 28000, SDS-PAGE Escherichia coli
107100
-
sequence determination Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
Escherichia coli

Reaction

Reaction Comment Organism Reaction ID
cholate + NAD+ = 3alpha,12alpha-dihydroxy-7-oxo-5beta-cholan-24-oate + NADH + H+ Tyr159 acts as basic catalyst, Lys163 binds to NAD(H) and lowers the pKa value of Tyr159, Ser146 stabilizes the substrate, reaction intermediate and product in catalysis Escherichia coli

Subunits

Subunits Comment Organism
tetramer 4 * 28000, SDS-PAGE Escherichia coli

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
7.92
-
cholic acid mutant K163I Escherichia coli
20.1
-
cholic acid mutant Y159H Escherichia coli
30.7
-
cholic acid mutant S146A Escherichia coli
53.7
-
cholic acid mutant S146H Escherichia coli
96.2
-
cholic acid mutant K163R Escherichia coli
151
-
cholic acid
-
Escherichia coli

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
10
-
oxidation of cholic acid Escherichia coli

pH Range

pH Minimum pH Maximum Comment Organism
6 10
-
Escherichia coli

Cofactor

Cofactor Comment Organism Structure
NAD+ wild type and mutants Escherichia coli