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Literature summary for 1.1.1.9 extracted from

  • Klimacek, M.; Hellmer, H.; Nidetzky, B.
    Catalytic mechanism of Zn2+-dependent polyol dehydrogenases: kinetic comparison of sheep liver sorbitol dehydrogenase with wild-type and Glu154-Cys forms of yeast xylitol dehydrogenase (2007), Biochem. J., 404, 421-429.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
expressed in Escherichia coli JM 109 Candida sp. HA 167

Protein Variants

Protein Variants Comment Organism
E154C mutant bearing a disrupted Zn2+ binding site: purified preparations show a variable Zn2+ (0.10-0.40 atom/subunit), mutant exhibits a constant catalytic Zn2+ centre activity and does not require exogenous Zn2+ for activity or stability. E154C retains 0.019% and 0.74% of wild-type catalytic efficiency (kcat/Km (sorbitol): 7800/Msec and kcat:161/sec) for NAD+-dependent oxidation of sorbitol at 25°C respectively. The pH profile of kcat/Ksorbitol for E154C decreases below an apparent pK of 9.1, reflecting a shift in pK by about +1.7-1.9 pH units compared with the corresponding pH profiles for wild-type. IC50 (ZnSO4): 0.005 mM Candida sp. HA 167

Inhibitors

Inhibitors Comment Organism Structure
Zn2+ exogenous Zn2+ (added as ZnSO4) in the concentration range 1-100 microM is a strong irreversible inhibitor of wild-type and mutant E154C Candida sp. HA 167
ZnSO4
-
Candida sp. HA 167

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3
-
D-sorbitol kcat/Km (sorbitol): 9500/Msec Ovis aries
21
-
sorbitol kcat/Km (sorbitol): 7800/Msec Candida sp. HA 167
290
-
NAD+ mutant E154C, kcat/Km (NAD+): 4100/Msec Candida sp. HA 167
430
-
NAD+ kcat/Km (NAD+): 370000/Msec Candida sp. HA 167
500
-
NAD+ kcat/Km (NAD+): 57000/Msec Ovis aries
785
-
sorbitol mutant E154C, kcat/Km (sorbitol): 1.5/Msec Candida sp. HA 167

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
160000
-
gel filtration, protein is a homotetramer Candida sp. HA 167

Organism

Organism UniProt Comment Textmining
Candida sp. HA 167
-
-
-
Ovis aries
-
-
-

Purification (Commentary)

Purification (Comment) Organism
using affinity chromatography and preparative gel filtration Candida sp. HA 167

Source Tissue

Source Tissue Comment Organism Textmining
liver
-
Ovis aries
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
D-sorbitol + NAD+
-
Ovis aries D-fructose + NADH + H+
-
r
sorbitol + NAD+
-
Candida sp. HA 167 D-fructose + NADH + H+
-
?
xylitol + NAD+
-
Ovis aries D-xylulose + NADH + H+
-
?
xylitol + NAD+
-
Candida sp. HA 167 D-xylulose + NADH + H+
-
?

Subunits

Subunits Comment Organism
homotetramer gel filtration Candida sp. HA 167

Synonyms

Synonyms Comment Organism
GmXDH
-
Candida sp. HA 167
slSDH
-
Ovis aries
xylitol dehydrogenase
-
Ovis aries
xylitol dehydrogenase
-
Candida sp. HA 167

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
25
-
assay at Ovis aries
25
-
assay at Candida sp. HA 167

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1.19
-
sorbitol mutant E154C Candida sp. HA 167
2 8 D-sorbitol
-
Ovis aries
161
-
sorbitol
-
Candida sp. HA 167

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
9
-
assay at Ovis aries
9
-
assay at Candida sp. HA 167

IC50 Value

IC50 Value IC50 Value Maximum Comment Organism Inhibitor Structure
0.005
-
value identical for wildtype and for mutant E154C Candida sp. HA 167 ZnSO4