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Literature summary 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)

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

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
1.1.1.10 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

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

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.1.1.10 0.002
-
 NADPH pH 7.0, 25°C, wild-type enzyme Homo sapiens
1.1.1.10 0.077
-
 diacetyl pH 7.0, 25°C, wild-type enzyme Homo sapiens
1.1.1.10 26
-
 diacetyl pH 7.0, 25°C, mutant N107D Homo sapiens
1.1.1.10 31
-
 diacetyl pH 7.0, 25°C, mutant N107L Homo sapiens
1.1.1.10 95
-
 NADPH pH 7.0, 25°C, mutant N107D Homo sapiens
1.1.1.10 97
-
 NADPH pH 7.0, 25°C, mutant N107L Homo sapiens

Natural Substrates/ Products (Substrates)

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

Organism

EC Number Organism UniProt Comment Textmining
1.1.1.10 Homo sapiens Q7Z4W1
-
-

Reaction

EC Number Reaction Comment Organism Reaction ID
1.1.1.10 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
a

Substrates and Products (Substrate)

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

Synonyms

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

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
1.1.1.10 25
-
 assay at Homo sapiens

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1.1.1.10 0.0008
-
 diacetyl pH 7.0, 25°C, mutant N107L Homo sapiens
1.1.1.10 0.009
-
 diacetyl pH 7.0, 25°C, mutant N107D Homo sapiens
1.1.1.10 1.57
-
 diacetyl pH 7.0, 25°C, wild-type enzyme Homo sapiens

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.1.1.10 7
-
 assay at Homo sapiens

Cofactor

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