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Literature summary for 1.1.1.9 extracted from

  • Han, X.; Hu, X.; Zhou, C.; Wang, H.; Li, Q.; Ouyang, Y.; Kuang, X.; Xiao, D.; Xiang, Q.; Yu, X.; Li, X.; Gu, Y.; Zhao, K.; Chen, Q.; Ma, M.
    Cloning and functional characterization of xylitol dehydrogenase genes from Issatchenkia orientalis and Torulaspora delbrueckii (2020), J. Biosci. Bioeng., 130, 29-35 .
    View publication on PubMed
Search for more literature for 1.1.1.9

Activating Compound

Activating Compound Comment Organism Structure
additional information glycerol has not a strong effect on the enzyme activity at 1-10 mM Scheffersomyces stipitis
additional information glycerol has not a strong effect on the enzyme activity at 1-10 mM Pichia kudriavzevii
additional information glycerol has not a strong effect on the enzyme activity at 1-10 mM Torulaspora delbrueckii
NaCl gradually activates the enzyme with increasing concentrations of 0.1-1.0 M Pichia kudriavzevii

Application

Application Comment Organism
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
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

Cloned(Commentary)

Cloned (Comment) Organism
gene Xyl2, DNA and amino acid sequence determination and analysis, sequence comparisons Pichia kudriavzevii

Inhibitors

Inhibitors Comment Organism Structure
2-mercaptoethanol slight inhibition Scheffersomyces stipitis
2-mercaptoethanol slight inhibition Torulaspora delbrueckii
EDTA strong inhibition at 1-10 mM Pichia kudriavzevii
EDTA strong inhibition at 1 mM, very strong inhibition at 5-10 mM Scheffersomyces stipitis
EDTA strong inhibition at 1-10 mM Torulaspora delbrueckii
KCl gradually inhibits the enzyme with increasing concentrations of 0.1-1.0 M Scheffersomyces stipitis
KCl gradually inhibits the enzyme with increasing concentrations of 0.1-1.0 M Torulaspora delbrueckii
Mg2+ slight inhibition Scheffersomyces stipitis
additional information glycerol has not a strong effect on the enzyme activity at 1-10 mM Pichia kudriavzevii
additional information glycerol has not a strong effect on the enzyme activity at 1-10 mM Scheffersomyces stipitis
additional information glycerol has not a strong effect on the enzyme activity at 1-10 mM Torulaspora delbrueckii
NaCl gradually inhibits the enzyme with increasing concentrations of 0.1-1.0 M Scheffersomyces stipitis
NaCl gradually inhibits the enzyme with increasing concentrations of 0.1-1.0 M Torulaspora delbrueckii

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
10.38
-
 xylitol pH 7.0, 30°C, recombinant enzyme Pichia kudriavzevii
17.64
-
 xylitol pH 7.0, 30°C, recombinant enzyme Scheffersomyces stipitis
20.96
-
 xylitol pH 7.0, 30°C, recombinant enzyme Torulaspora delbrueckii

Localization

Localization Comment Organism GeneOntology No. Textmining
cytoplasm
-
 Scheffersomyces stipitis 5737
-
cytoplasm
-
 Pichia kudriavzevii 5737
-
cytoplasm
-
 Torulaspora delbrueckii 5737
-

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ activates Pichia kudriavzevii
Mg2+ activates Torulaspora delbrueckii
additional information KCl has not a strong effect on the enzyme activity at 0.1-1.0 Pichia kudriavzevii

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
xylitol + NAD+ Scheffersomyces stipitis
-
 D-xylulose + NADH + H+
-
 r
xylitol + NAD+ Pichia kudriavzevii
-
 D-xylulose + NADH + H+
-
 r
xylitol + NAD+ Torulaspora delbrueckii
-
 D-xylulose + NADH + H+
-
 r
xylitol + NAD+ Pichia kudriavzevii QLB_09
-
 D-xylulose + NADH + H+
-
 r
xylitol + NAD+ Scheffersomyces stipitis NRRL Y-11545
-
 D-xylulose + NADH + H+
-
 r
xylitol + NAD+ Scheffersomyces stipitis NBRC 10063
-
 D-xylulose + NADH + H+
-
 r
xylitol + NAD+ Scheffersomyces stipitis ATCC 58785
-
 D-xylulose + NADH + H+
-
 r
xylitol + NAD+ Torulaspora delbrueckii BLQ_03
-
 D-xylulose + NADH + H+
-
 r

Organism

Organism UniProt Comment Textmining
Pichia kudriavzevii A0A3S7PMB5 Issatchenkia orientalis, a multistress-tolerant yeast
-
Pichia kudriavzevii QLB_09 A0A3S7PMB5 Issatchenkia orientalis, a multistress-tolerant yeast
-
Scheffersomyces stipitis P22144 Pichia stipitis
-
Scheffersomyces stipitis ATCC 58785 P22144 Pichia stipitis
-
Scheffersomyces stipitis NBRC 10063 P22144 Pichia stipitis
-
Scheffersomyces stipitis NRRL Y-11545 P22144 Pichia stipitis
-
Torulaspora delbrueckii A0A3S7PMC4 Candida colliculosa, a multistress-tolerant yeast
-
Torulaspora delbrueckii BLQ_03 A0A3S7PMC4 Candida colliculosa, a multistress-tolerant yeast
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
10.71
-
 pH 7.0, 30°C, recombinant enzyme with xylitol and NAD+ as substrates Torulaspora delbrueckii
13.29
-
 pH 7.0, 30°C, recombinant enzyme with xylitol and NAD+ as substrates Scheffersomyces stipitis
14.66
-
 pH 7.0, 30°C, recombinant enzyme with xylitol and NAD+ as substrates Pichia kudriavzevii

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
xylitol + NAD+
-
 Scheffersomyces stipitis D-xylulose + NADH + H+
-
 r
xylitol + NAD+
-
 Pichia kudriavzevii D-xylulose + NADH + H+
-
 r
xylitol + NAD+
-
 Torulaspora delbrueckii D-xylulose + NADH + H+
-
 r
xylitol + NAD+
-
 Pichia kudriavzevii QLB_09 D-xylulose + NADH + H+
-
 r
xylitol + NAD+
-
 Scheffersomyces stipitis NRRL Y-11545 D-xylulose + NADH + H+
-
 r
xylitol + NAD+
-
 Scheffersomyces stipitis NBRC 10063 D-xylulose + NADH + H+
-
 r
xylitol + NAD+
-
 Scheffersomyces stipitis ATCC 58785 D-xylulose + NADH + H+
-
 r
xylitol + NAD+
-
 Torulaspora delbrueckii BLQ_03 D-xylulose + NADH + H+
-
 r

Subunits

Subunits Comment Organism
? x * 38000, SDS-PAGE Torulaspora delbrueckii
? x * 38500, SDS-PAGE Scheffersomyces stipitis
? x * 40100, SDS-PAGE Pichia kudriavzevii

Synonyms

Synonyms Comment Organism
IoXyl2p
-
 Pichia kudriavzevii
SsXyl2p
-
 Scheffersomyces stipitis
TdXyl2p
-
 Torulaspora delbrueckii
XDH
-
 Scheffersomyces stipitis
XDH
-
 Pichia kudriavzevii
XDH
-
 Torulaspora delbrueckii
XYL2
-
 Scheffersomyces stipitis
XYL2
-
 Pichia kudriavzevii
XYL2
-
 Torulaspora delbrueckii

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
35
-
 oxidation of xylitol Scheffersomyces stipitis
35
-
 oxidation of xylitol Torulaspora delbrueckii
45
-
 oxidation of xylitol Pichia kudriavzevii

Temperature Range [°C]

Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
20 55 over 40% of maximal activity within this range, profile overview Scheffersomyces stipitis
25 60 over 40% of maximal activity within this range, profile overview Pichia kudriavzevii
25 55 over 40% of maximal activity within this range, profile overview Torulaspora delbrueckii

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
13.28
-
 xylitol pH 7.0, 30°C, recombinant enzyme Torulaspora delbrueckii
15.015
-
 xylitol pH 7.0, 30°C, recombinant enzyme Pichia kudriavzevii
19.62
-
 xylitol pH 7.0, 30°C, recombinant enzyme Scheffersomyces stipitis

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.5
-
 oxidation of xylitol Scheffersomyces stipitis
8
-
 oxidation of xylitol Pichia kudriavzevii
8.5
-
 oxidation of xylitol Torulaspora delbrueckii

pH Range

pH Minimum pH Maximum Comment Organism
5.5 9 over 50% of maximal activity within this range, profile overview Scheffersomyces stipitis
6 9 over 50% of maximal activity within this range, profile overview Pichia kudriavzevii
6.5 9 over 50% of maximal activity within this range, profile overview Torulaspora delbrueckii

Cofactor

Cofactor Comment Organism Structure
NAD+ strictly dependent on Scheffersomyces stipitis
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
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
NADH
-
 Scheffersomyces stipitis
NADH
-
 Pichia kudriavzevii
NADH
-
 Torulaspora delbrueckii

General Information

General Information Comment Organism
additional information enzyme IoXyl2p ahs the conserved domain GxGxxG (Gly188-Gly190-Gly193 in IoXyl2p) for cofactor binding Pichia kudriavzevii
additional information enzyme TdXyl2p has the conserved domain GxGxxG (Gly176-Gly178-Gly181 in TdXyl2p) for cofactor binding Torulaspora delbrueckii

kcat/KM [mM/s]

kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
1.024
-
 xylitol pH 7.0, 30°C, recombinant enzyme Pichia kudriavzevii
1.11
-
 xylitol pH 7.0, 30°C, recombinant enzyme Scheffersomyces stipitis
1.24
-
 xylitol pH 7.0, 30°C, recombinant enzyme Torulaspora delbrueckii