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Literature summary for 1.1.1.10 extracted from

  • Ishikura, S.; Isaji, T.; Usami, N.; Nakagawa, J.; El-Kabbani, O.; Hara, A.
    Identification of amino acid residues involved in substrate recognition of L-xylulose reductase by site-directed mutagenesis (2003), Chem. Biol. Interact., 143-144, 543-550.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
expression of wild-type and mutant enzymes in Escherichia coli Rattus norvegicus

Protein Variants

Protein Variants Comment Organism
H146L site-directed mutagenesis, altered activity Rattus norvegicus
K153M site-directed mutagenesis, active site mutant, complete loss of activity Rattus norvegicus
L143F site-directed mutagenesis, altered activity Rattus norvegicus
N190V site-directed mutagenesis, altered activity Rattus norvegicus
N190V/W191S site-directed mutagenesis, almost complete loss of L-xylulose reductase activity Rattus norvegicus
N190V/W191S/Q137M/L143F/H146L site-directed mutagenesis, almost complete loss of L-xylulose reductase activity, mutant shows high 3-ketosteroid reductase activity Rattus norvegicus
Q137M site-directed mutagenesis, altered activity, stable against cold inactivation Rattus norvegicus
Q137M/F241L site-directed mutagenesis, altered activity, sensitive to cold inactivation like the wild-type enzyme Rattus norvegicus
Q137M/L143F site-directed mutagenesis, increased Km for L-xylulose compared to the wild-type Rattus norvegicus
Q137M/L143F/H146L site-directed mutagenesis, almost complete loss of L-xylulose reductase activity, mutant shows 3-ketosteroid reductase activity Rattus norvegicus
S136A site-directed mutagenesis, active site mutant, complete loss of activity Rattus norvegicus
W191F site-directed mutagenesis, altered activity Rattus norvegicus
W191S site-directed mutagenesis, altered activity Rattus norvegicus
Y149F site-directed mutagenesis, active site mutant, complete loss of activity Rattus norvegicus

Inhibitors

Inhibitors Comment Organism Structure
n-butyric acid specific, binds to the enzyme-NADP+ complex, the mutant enzymes show altered sensitivity to inhibition, overview Rattus norvegicus

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.00067
-
NADP+ pH 7.0, 25°C, mutant S136A Rattus norvegicus
0.0013
-
NADP+ pH 7.0, 25°C, mutant Y149F Rattus norvegicus
0.002
-
NADPH pH 7.0, 25°C, mutant Y149F Rattus norvegicus
0.003
-
NADP+ pH 7.0, 25°C, wild-type enzyme Rattus norvegicus
0.0046
-
NADPH pH 7.0, 25°C, mutant S136A Rattus norvegicus
0.005
-
1,4-dibromo-2,3-butanedione pH 7.0, 25°C, wild-type enzyme Rattus norvegicus
0.007
-
NADPH pH 7.0, 25°C, wild-type enzyme Rattus norvegicus
0.0099
-
L-xylitol pH 7.0, 25°C, mutant Y149F Rattus norvegicus
0.011
-
L-xylitol pH 7.0, 25°C, wild-type enzyme Rattus norvegicus
0.013
-
L-xylitol pH 7.0, 25°C, mutant S136A Rattus norvegicus
0.05
-
1,4-dibromo-2,3-butanedione pH 7.0, 25°C, mutant S136A Rattus norvegicus
0.053
-
NADPH pH 7.0, 25°C, mutant K153M Rattus norvegicus
0.085
-
L-xylitol pH 7.0, 25°C, mutant K153M Rattus norvegicus
0.092
-
L-xylulose pH 7.0, 25°C, mutant H146L Rattus norvegicus
0.1
-
1,4-dibromo-2,3-butanedione pH 7.0, 25°C, mutant K153M Rattus norvegicus
0.117
-
NADP+ pH 7.0, 25°C, mutant K153M Rattus norvegicus
0.139
-
1,4-dibromo-2,3-butanedione pH 7.0, 25°C, mutant Y149F Rattus norvegicus
0.14
-
L-xylulose pH 7.0, 25°C, wild-type enzyme and mutant L143F Rattus norvegicus
0.31
-
L-xylulose pH 7.0, 25°C, mutant N190V Rattus norvegicus
0.33
-
L-xylulose pH 7.0, 25°C, mutant Q137M Rattus norvegicus
0.78
-
diacetyl pH 7.0, 25°C, wild-type enzyme Rattus norvegicus
1.2
-
diacetyl pH 7.0, 25°C, mutant H146L Rattus norvegicus
2.6
-
diacetyl pH 7.0, 25°C, mutant N190V Rattus norvegicus
2.7
-
diacetyl pH 7.0, 25°C, mutant N190V/W191S/Q137M/L143F/H146L Rattus norvegicus
3
-
diacetyl pH 7.0, 25°C, mutant Q137M Rattus norvegicus
3.6
-
L-xylulose pH 7.0, 25°C, mutant Q137M/L143F Rattus norvegicus
5.2
-
diacetyl pH 7.0, 25°C, mutant W191F Rattus norvegicus
6.2
-
diacetyl pH 7.0, 25°C, mutant L143F Rattus norvegicus
7.2
-
L-xylulose pH 7.0, 25°C, mutant W191F Rattus norvegicus
9.6
-
diacetyl pH 7.0, 25°C, mutant Q137M/L143F/H146L Rattus norvegicus
11
-
diacetyl pH 7.0, 25°C, mutant Q137M/L143F Rattus norvegicus
16
-
diacetyl pH 7.0, 25°C, mutant N190V/W191S Rattus norvegicus
42
-
diacetyl pH 7.0, 25°C, mutant W191S Rattus norvegicus

Localization

Localization Comment Organism GeneOntology No. Textmining
membrane
-
Rattus norvegicus 16020
-

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
26500
-
x * 26500 Rattus norvegicus

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
diacetyl + NAD(P)H Rattus norvegicus detoxification of alpha-dicarbonyl compounds acetoin + NAD(P)+
-
r
L-xylulose + NADPH + H+ Rattus norvegicus part of the uronate cycle, involved in osmoregulation in the kidney L-xylitol + NADP+
-
r

Organism

Organism UniProt Comment Textmining
Rattus norvegicus
-
-
-

Reaction

Reaction Comment Organism Reaction ID
xylitol + NADP+ = L-xylulose + NADPH + H+ enzyme with dual function showing L-xylulose reductase and dicarbonyl reductase activities, it is probably identical with sperm 34 kDa protein P34H and diacetyl reductase, EC 1.1.1.5, the amino acid residues Ser136, Tyr149, and Lys153 form the catalytic triad Rattus norvegicus

Source Tissue

Source Tissue Comment Organism Textmining
kidney brush border Rattus norvegicus
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1,4-dibromo-2,3-butanedione + NADPH dicarbonyl reductase activity Rattus norvegicus ? + NADP+
-
r
diacetyl + NAD(P)H detoxification of alpha-dicarbonyl compounds Rattus norvegicus acetoin + NAD(P)+
-
r
diacetyl + NAD(P)H dicarbonyl reductase activity Rattus norvegicus acetoin + NAD(P)+
-
r
L-xylulose + NADPH + H+ part of the uronate cycle, involved in osmoregulation in the kidney Rattus norvegicus L-xylitol + NADP+
-
r
L-xylulose + NADPH + H+ L-xylulose reductase activity Rattus norvegicus L-xylitol + NADP+
-
r
additional information the size and hydrophobicity of the amino acid residues involved in substrate recognition, i.e. Q137, L143, H146, N190, and W191, is important, mutants N190V, N190V/W191S, Q137M/L143F/H146L, and N190V/W191S/Q137M/L143F/H146L show reductive activity with 4-nitroacetophenone, 5beta-androstane-3,17-dione, 5beta-androstan-17beta-ol-3-one, and 5beta-androstane-3alpha,17beta-diol, overview Rattus norvegicus ?
-
?

Subunits

Subunits Comment Organism
? x * 26500 Rattus norvegicus

Synonyms

Synonyms Comment Organism
More enzyme belongs to the short-chain dehydrogenase/reductase family Rattus norvegicus
XR
-
Rattus norvegicus

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
25
-
assay at Rattus norvegicus

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.0005
-
NADPH pH 7.0, 25°C, mutant K153M Rattus norvegicus
0.0006
-
NADPH pH 7.0, 25°C, mutant S136A Rattus norvegicus
0.0009
-
NADPH pH 7.0, 25°C, mutant Y149F Rattus norvegicus
9.5
-
NADP+ pH 7.0, 25°C, wild-type enzyme Rattus norvegicus
25
-
NADPH pH 7.0, 25°C, wild-type enzyme Rattus norvegicus

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7
-
assay at Rattus norvegicus

Cofactor

Cofactor Comment Organism Structure
NADP+
-
Rattus norvegicus
NADPH
-
Rattus norvegicus