EC Number | Activating Compound | Comment | Organism | Structure |
---|---|---|---|---|
1.1.1.9 | additional information | glycerol has not a strong effect on the enzyme activity at 1-10 mM | Scheffersomyces stipitis | |
1.1.1.9 | additional information | glycerol has not a strong effect on the enzyme activity at 1-10 mM | Pichia kudriavzevii | |
1.1.1.9 | additional information | glycerol has not a strong effect on the enzyme activity at 1-10 mM | Torulaspora delbrueckii | |
1.1.1.9 | NaCl | gradually activates the enzyme with increasing concentrations of 0.1-1.0 M | Pichia kudriavzevii |
EC Number | Application | Comment | Organism |
---|---|---|---|
1.1.1.9 | synthesis | enzyme IoXyl2p from Issatchenkia orientalis is considered to be an attractive candidate for the construction of genetically engineered Saccharomyces cerevisiae for efficient fermentation of carbohydrate in lignocellulosic hydrolysate | Pichia kudriavzevii |
1.1.1.9 | synthesis | enzyme TdXyl2p from Torulaspora delbrueckii is considered to be an attractive candidate for the construction of genetically engineered Saccharomyces cerevisiae for efficient fermentation of carbohydrate in lignocellulosic hydrolysate | Torulaspora delbrueckii |
EC Number | Cloned (Comment) | Organism |
---|---|---|
1.1.1.9 | gene Xyl2, DNA and amino acid sequence determination and analysis, sequence comparisons | Pichia kudriavzevii |
EC Number | Inhibitors | Comment | Organism | Structure |
---|---|---|---|---|
1.1.1.9 | 2-mercaptoethanol | slight inhibition | Scheffersomyces stipitis | |
1.1.1.9 | 2-mercaptoethanol | slight inhibition | Torulaspora delbrueckii | |
1.1.1.9 | EDTA | strong inhibition at 1-10 mM | Pichia kudriavzevii | |
1.1.1.9 | EDTA | strong inhibition at 1 mM, very strong inhibition at 5-10 mM | Scheffersomyces stipitis | |
1.1.1.9 | EDTA | strong inhibition at 1-10 mM | Torulaspora delbrueckii | |
1.1.1.9 | KCl | gradually inhibits the enzyme with increasing concentrations of 0.1-1.0 M | Scheffersomyces stipitis | |
1.1.1.9 | KCl | gradually inhibits the enzyme with increasing concentrations of 0.1-1.0 M | Torulaspora delbrueckii | |
1.1.1.9 | Mg2+ | slight inhibition | Scheffersomyces stipitis | |
1.1.1.9 | additional information | glycerol has not a strong effect on the enzyme activity at 1-10 mM | Pichia kudriavzevii | |
1.1.1.9 | additional information | glycerol has not a strong effect on the enzyme activity at 1-10 mM | Scheffersomyces stipitis | |
1.1.1.9 | additional information | glycerol has not a strong effect on the enzyme activity at 1-10 mM | Torulaspora delbrueckii | |
1.1.1.9 | NaCl | gradually inhibits the enzyme with increasing concentrations of 0.1-1.0 M | Scheffersomyces stipitis | |
1.1.1.9 | NaCl | gradually inhibits the enzyme with increasing concentrations of 0.1-1.0 M | Torulaspora delbrueckii |
EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
1.1.1.9 | 10.38 | - |
xylitol | pH 7.0, 30°C, recombinant enzyme | Pichia kudriavzevii | |
1.1.1.9 | 17.64 | - |
xylitol | pH 7.0, 30°C, recombinant enzyme | Scheffersomyces stipitis | |
1.1.1.9 | 20.96 | - |
xylitol | pH 7.0, 30°C, recombinant enzyme | Torulaspora delbrueckii |
EC Number | Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|---|
1.1.1.9 | cytoplasm | - |
Scheffersomyces stipitis | 5737 | - |
1.1.1.9 | cytoplasm | - |
Pichia kudriavzevii | 5737 | - |
1.1.1.9 | cytoplasm | - |
Torulaspora delbrueckii | 5737 | - |
EC Number | Metals/Ions | Comment | Organism | Structure |
---|---|---|---|---|
1.1.1.9 | Mg2+ | activates | Pichia kudriavzevii | |
1.1.1.9 | Mg2+ | activates | Torulaspora delbrueckii | |
1.1.1.9 | additional information | KCl has not a strong effect on the enzyme activity at 0.1-1.0 | Pichia kudriavzevii |
EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
1.1.1.9 | xylitol + NAD+ | Scheffersomyces stipitis | - |
D-xylulose + NADH + H+ | - |
r | |
1.1.1.9 | xylitol + NAD+ | Pichia kudriavzevii | - |
D-xylulose + NADH + H+ | - |
r | |
1.1.1.9 | xylitol + NAD+ | Torulaspora delbrueckii | - |
D-xylulose + NADH + H+ | - |
r | |
1.1.1.9 | xylitol + NAD+ | Pichia kudriavzevii QLB_09 | - |
D-xylulose + NADH + H+ | - |
r | |
1.1.1.9 | xylitol + NAD+ | Scheffersomyces stipitis NRRL Y-11545 | - |
D-xylulose + NADH + H+ | - |
r | |
1.1.1.9 | xylitol + NAD+ | Scheffersomyces stipitis NBRC 10063 | - |
D-xylulose + NADH + H+ | - |
r | |
1.1.1.9 | xylitol + NAD+ | Scheffersomyces stipitis ATCC 58785 | - |
D-xylulose + NADH + H+ | - |
r | |
1.1.1.9 | xylitol + NAD+ | Torulaspora delbrueckii BLQ_03 | - |
D-xylulose + NADH + H+ | - |
r |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
1.1.1.9 | Pichia kudriavzevii | A0A3S7PMB5 | Issatchenkia orientalis, a multistress-tolerant yeast | - |
1.1.1.9 | Pichia kudriavzevii QLB_09 | A0A3S7PMB5 | Issatchenkia orientalis, a multistress-tolerant yeast | - |
1.1.1.9 | Scheffersomyces stipitis | P22144 | Pichia stipitis | - |
1.1.1.9 | Scheffersomyces stipitis ATCC 58785 | P22144 | Pichia stipitis | - |
1.1.1.9 | Scheffersomyces stipitis NBRC 10063 | P22144 | Pichia stipitis | - |
1.1.1.9 | Scheffersomyces stipitis NRRL Y-11545 | P22144 | Pichia stipitis | - |
1.1.1.9 | Torulaspora delbrueckii | A0A3S7PMC4 | Candida colliculosa, a multistress-tolerant yeast | - |
1.1.1.9 | Torulaspora delbrueckii BLQ_03 | A0A3S7PMC4 | Candida colliculosa, a multistress-tolerant yeast | - |
EC Number | Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
---|---|---|---|---|
1.1.1.9 | 10.71 | - |
pH 7.0, 30°C, recombinant enzyme with xylitol and NAD+ as substrates | Torulaspora delbrueckii |
1.1.1.9 | 13.29 | - |
pH 7.0, 30°C, recombinant enzyme with xylitol and NAD+ as substrates | Scheffersomyces stipitis |
1.1.1.9 | 14.66 | - |
pH 7.0, 30°C, recombinant enzyme with xylitol and NAD+ as substrates | Pichia kudriavzevii |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
1.1.1.9 | xylitol + NAD+ | - |
Scheffersomyces stipitis | D-xylulose + NADH + H+ | - |
r | |
1.1.1.9 | xylitol + NAD+ | - |
Pichia kudriavzevii | D-xylulose + NADH + H+ | - |
r | |
1.1.1.9 | xylitol + NAD+ | - |
Torulaspora delbrueckii | D-xylulose + NADH + H+ | - |
r | |
1.1.1.9 | xylitol + NAD+ | - |
Pichia kudriavzevii QLB_09 | D-xylulose + NADH + H+ | - |
r | |
1.1.1.9 | xylitol + NAD+ | - |
Scheffersomyces stipitis NRRL Y-11545 | D-xylulose + NADH + H+ | - |
r | |
1.1.1.9 | xylitol + NAD+ | - |
Scheffersomyces stipitis NBRC 10063 | D-xylulose + NADH + H+ | - |
r | |
1.1.1.9 | xylitol + NAD+ | - |
Scheffersomyces stipitis ATCC 58785 | D-xylulose + NADH + H+ | - |
r | |
1.1.1.9 | xylitol + NAD+ | - |
Torulaspora delbrueckii BLQ_03 | D-xylulose + NADH + H+ | - |
r |
EC Number | Subunits | Comment | Organism |
---|---|---|---|
1.1.1.9 | ? | x * 38000, SDS-PAGE | Torulaspora delbrueckii |
1.1.1.9 | ? | x * 38500, SDS-PAGE | Scheffersomyces stipitis |
1.1.1.9 | ? | x * 40100, SDS-PAGE | Pichia kudriavzevii |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
1.1.1.9 | IoXyl2p | - |
Pichia kudriavzevii |
1.1.1.9 | SsXyl2p | - |
Scheffersomyces stipitis |
1.1.1.9 | TdXyl2p | - |
Torulaspora delbrueckii |
1.1.1.9 | XDH | - |
Scheffersomyces stipitis |
1.1.1.9 | XDH | - |
Pichia kudriavzevii |
1.1.1.9 | XDH | - |
Torulaspora delbrueckii |
1.1.1.9 | XYL2 | - |
Scheffersomyces stipitis |
1.1.1.9 | XYL2 | - |
Pichia kudriavzevii |
1.1.1.9 | XYL2 | - |
Torulaspora delbrueckii |
EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|---|
1.1.1.9 | 35 | - |
oxidation of xylitol | Scheffersomyces stipitis |
1.1.1.9 | 35 | - |
oxidation of xylitol | Torulaspora delbrueckii |
1.1.1.9 | 45 | - |
oxidation of xylitol | Pichia kudriavzevii |
EC Number | Temperature Minimum [°C] | Temperature Maximum [°C] | Comment | Organism |
---|---|---|---|---|
1.1.1.9 | 20 | 55 | over 40% of maximal activity within this range, profile overview | Scheffersomyces stipitis |
1.1.1.9 | 25 | 60 | over 40% of maximal activity within this range, profile overview | Pichia kudriavzevii |
1.1.1.9 | 25 | 55 | over 40% of maximal activity within this range, profile overview | Torulaspora delbrueckii |
EC Number | Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
1.1.1.9 | 13.28 | - |
xylitol | pH 7.0, 30°C, recombinant enzyme | Torulaspora delbrueckii | |
1.1.1.9 | 15.015 | - |
xylitol | pH 7.0, 30°C, recombinant enzyme | Pichia kudriavzevii | |
1.1.1.9 | 19.62 | - |
xylitol | pH 7.0, 30°C, recombinant enzyme | Scheffersomyces stipitis |
EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|---|
1.1.1.9 | 7.5 | - |
oxidation of xylitol | Scheffersomyces stipitis |
1.1.1.9 | 8 | - |
oxidation of xylitol | Pichia kudriavzevii |
1.1.1.9 | 8.5 | - |
oxidation of xylitol | Torulaspora delbrueckii |
EC Number | pH Minimum | pH Maximum | Comment | Organism |
---|---|---|---|---|
1.1.1.9 | 5.5 | 9 | over 50% of maximal activity within this range, profile overview | Scheffersomyces stipitis |
1.1.1.9 | 6 | 9 | over 50% of maximal activity within this range, profile overview | Pichia kudriavzevii |
1.1.1.9 | 6.5 | 9 | over 50% of maximal activity within this range, profile overview | Torulaspora delbrueckii |
EC Number | Cofactor | Comment | Organism | Structure |
---|---|---|---|---|
1.1.1.9 | NAD+ | strictly dependent on | Scheffersomyces stipitis | |
1.1.1.9 | NAD+ | strictly dependent on, residues Val180, Asp200, and Lys205 are responsible for NAD+ binding. Especially, Asp200 in TdXyl2p determines the specificity for NAD+, which forms double-hydrogen bonds to the hydroxyl groups in the ribosyl moiety of NAD+ | Torulaspora delbrueckii | |
1.1.1.9 | NAD+ | strictly dependent on, residues Val192, Asp212, and Lys217 are responsible for NAD+ binding. Especially, Asp212 in IoXyl2p determines the specificity for NAD+, which forms double-hydrogen bonds to the hydroxyl groups in the ribosyl moiety of NAD+ | Pichia kudriavzevii | |
1.1.1.9 | NADH | - |
Scheffersomyces stipitis | |
1.1.1.9 | NADH | - |
Pichia kudriavzevii | |
1.1.1.9 | NADH | - |
Torulaspora delbrueckii |
EC Number | General Information | Comment | Organism |
---|---|---|---|
1.1.1.9 | additional information | enzyme IoXyl2p ahs the conserved domain GxGxxG (Gly188-Gly190-Gly193 in IoXyl2p) for cofactor binding | Pichia kudriavzevii |
1.1.1.9 | additional information | enzyme TdXyl2p has the conserved domain GxGxxG (Gly176-Gly178-Gly181 in TdXyl2p) for cofactor binding | Torulaspora delbrueckii |
EC Number | kcat/KM Value [1/mMs-1] | kcat/KM Value Maximum [1/mMs-1] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
1.1.1.9 | 1.024 | - |
xylitol | pH 7.0, 30°C, recombinant enzyme | Pichia kudriavzevii | |
1.1.1.9 | 1.11 | - |
xylitol | pH 7.0, 30°C, recombinant enzyme | Scheffersomyces stipitis | |
1.1.1.9 | 1.24 | - |
xylitol | pH 7.0, 30°C, recombinant enzyme | Torulaspora delbrueckii |