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Literature summary for 1.1.1.10 extracted from

  • El-Kabbani, O.; Ishikura, S.; Darmanin, C.; Carbone, V.; Chung, R.P.T.; Usami, N.; Hara, A.
    Crystal structure of human L-xylulose reductase holoenzyme: probing the role of Asn107 with site-directed mutagenesis (2004), Proteins, 55, 724-732.
    View publication on PubMed

Cloned(Commentary)

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

Crystallization (Commentary)

Crystallization (Comment) Organism
18 mg/ml purified enzyme complexed with NADPH, in 10 mM Tris-HCl, pH 7.5, 2 mM 2-mercaptoethanol, 20% glycerol, replacement buffer is 10 mM Tris-HCl, pH 7.5, 2 mM 2-mercaptoethanol, mixed with 12.9 mM NADPH, in a molar ratio of enzyme and cofactor of 1:8, equal volume of 0.003 ml of enzyme complex mixture and well solution, containing 15% PEG 8000, 50 mM potassium phosphate, and 0.1 M MES, pH 6.5, 1 week, X-ray diffraction structure determination and analysis, molecular replacement method, 1.96 A resolution, molecular modeling Homo sapiens

Protein Variants

Protein Variants Comment Organism
N107D site-directed mutagenesis, active site residue mutant, inactive Homo sapiens
N107L site-directed mutagenesis, active site residue mutant, inactive Homo sapiens

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.002
-
NADPH pH 7.0, 25°C, wild-type enzyme Homo sapiens
0.077
-
diacetyl pH 7.0, 25°C, wild-type enzyme Homo sapiens
26
-
diacetyl pH 7.0, 25°C, mutant N107D Homo sapiens
31
-
diacetyl pH 7.0, 25°C, mutant N107L Homo sapiens
95
-
NADPH pH 7.0, 25°C, mutant N107D Homo sapiens
97
-
NADPH pH 7.0, 25°C, mutant N107L Homo sapiens

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
L-xylulose + NADPH + H+ Homo sapiens the enzyme is involved in the uronate cycle of glucose metabolism L-xylitol + NADP+
-
r

Organism

Organism UniProt Comment Textmining
Homo sapiens Q7Z4W1
-
-

Reaction

Reaction Comment Organism Reaction ID
xylitol + NADP+ = L-xylulose + NADPH + H+ active site residues are Cys138, Val143, His146, Trp191, and Met200, the catalytic tetrad is formed by Asn107, Ser136, Tyr149, and Lys153, substrate binding site structure, enzyme with dual function showing L-xylulose reductase activity and dicarbonyl reductase activity, EC 1.1.1.5 Homo sapiens

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
diacetyl + NAD(P)H dicarbonyl reductase activity Homo sapiens acetoin + NAD(P)+
-
r
L-xylulose + NADPH + H+ the enzyme is involved in the uronate cycle of glucose metabolism Homo sapiens L-xylitol + NADP+
-
r
L-xylulose + NADPH + H+ L-xylulose reductase activity Homo sapiens L-xylitol + NADP+
-
r

Synonyms

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

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
25
-
assay at Homo sapiens

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.0008
-
diacetyl pH 7.0, 25°C, mutant N107L Homo sapiens
0.009
-
diacetyl pH 7.0, 25°C, mutant N107D Homo sapiens
1.57
-
diacetyl pH 7.0, 25°C, wild-type enzyme Homo sapiens

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7
-
assay at Homo sapiens

Cofactor

Cofactor Comment Organism Structure
NADP+ binding structure determination Homo sapiens
NADPH binding structure determination Homo sapiens