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show all sequences of 1.1.1.265

Structural insights into the cofactor-assisted substrate recognition of yeast methylglyoxal/isovaleraldehyde reductase Gre2

Guo, P.C.; Bao, Z.Z.; Ma, X.X.; Xia, Q.; Li, W.F.; Biochim. Biophys. Acta 1844, 1486-1492 (2014)

Data extracted from this reference:

Cloned(Commentary)
Commentary
Organism
expression in Escherichia coli
Saccharomyces cerevisiae
Crystallization (Commentary)
Crystallization
Organism
crystal structures in an apo-form at 2.00 A and NADPH-complexed form at 2.40 A resolution. Gre2 forms a homodimer, each subunit of which contains an N-terminal Rossmann-fold domain and a variable C-terminal domain, which participates in substrate recognition. The induced fit upon binding to the cofactor NADPH makes the two domains shift toward each other, producing an interdomain cleft that better fits the substrate
Saccharomyces cerevisiae
Engineering
Amino acid exchange
Commentary
Organism
F132A
about 200% of wild-type activity
Saccharomyces cerevisiae
F85A
less than 0.5% of wild-type activity
Saccharomyces cerevisiae
L169L
complete loss of activity
Saccharomyces cerevisiae
S127A
complete loss of activity
Saccharomyces cerevisiae
V162A
about 150% of wild-type activity
Saccharomyces cerevisiae
V198A
about 1.5% of wild-type activity
Saccharomyces cerevisiae
Y128A
about 1.5% of wild-type activity
Saccharomyces cerevisiae
Y128F
activity similar to wild-type
Saccharomyces cerevisiae
Y165A
complete loss of activity
Saccharomyces cerevisiae
Y165F
complete loss of activity
Saccharomyces cerevisiae
Y198F
about 75% of wild-type activity
Saccharomyces cerevisiae
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.12
-
3-Methylbutanal
mutant Y198F, pH 7.5, 30°C
Saccharomyces cerevisiae
0.14
-
3-Methylbutanal
wild-type, pH 7.5, 30°C
Saccharomyces cerevisiae
0.18
-
3-Methylbutanal
mutant F132A, pH 7.5, 30°C
Saccharomyces cerevisiae
0.2
-
3-Methylbutanal
mutant V162A, pH 7.5, 30°C
Saccharomyces cerevisiae
0.23
-
3-Methylbutanal
mutant Y128F, pH 7.5, 30°C
Saccharomyces cerevisiae
0.67
-
3-Methylbutanal
mutant Y128A, pH 7.5, 30°C
Saccharomyces cerevisiae
4.1
-
3-Methylbutanal
mutant Y198A, pH 7.5, 30°C
Saccharomyces cerevisiae
11.1
-
3-Methylbutanal
mutant F85A, pH 7.5, 30°C
Saccharomyces cerevisiae
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Saccharomyces cerevisiae
Q12068
cf. EC 1.1.1.283
-
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
3-methylbutanal + NAD(P)H + H+
-
737753
Saccharomyces cerevisiae
3-methylbutanol + NAD(P)+
-
-
-
r
Turnover Number [1/s]
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
1.4
-
3-Methylbutanal
mutant Y128A, pH 7.5, 30°C
Saccharomyces cerevisiae
5.9
-
3-Methylbutanal
mutant F85A, pH 7.5, 30°C
Saccharomyces cerevisiae
9.3
-
3-Methylbutanal
mutant Y198A, pH 7.5, 30°C
Saccharomyces cerevisiae
15.5
-
3-Methylbutanal
mutant Y198F, pH 7.5, 30°C
Saccharomyces cerevisiae
23.2
-
3-Methylbutanal
wild-type, pH 7.5, 30°C
Saccharomyces cerevisiae
38.9
-
3-Methylbutanal
mutant Y128F, pH 7.5, 30°C
Saccharomyces cerevisiae
52.6
-
3-Methylbutanal
mutant V162A, pH 7.5, 30°C
Saccharomyces cerevisiae
62.4
-
3-Methylbutanal
mutant F132A, pH 7.5, 30°C
Saccharomyces cerevisiae
Cloned(Commentary) (protein specific)
Commentary
Organism
expression in Escherichia coli
Saccharomyces cerevisiae
Crystallization (Commentary) (protein specific)
Crystallization
Organism
crystal structures in an apo-form at 2.00 A and NADPH-complexed form at 2.40 A resolution. Gre2 forms a homodimer, each subunit of which contains an N-terminal Rossmann-fold domain and a variable C-terminal domain, which participates in substrate recognition. The induced fit upon binding to the cofactor NADPH makes the two domains shift toward each other, producing an interdomain cleft that better fits the substrate
Saccharomyces cerevisiae
Engineering (protein specific)
Amino acid exchange
Commentary
Organism
F132A
about 200% of wild-type activity
Saccharomyces cerevisiae
F85A
less than 0.5% of wild-type activity
Saccharomyces cerevisiae
L169L
complete loss of activity
Saccharomyces cerevisiae
S127A
complete loss of activity
Saccharomyces cerevisiae
V162A
about 150% of wild-type activity
Saccharomyces cerevisiae
V198A
about 1.5% of wild-type activity
Saccharomyces cerevisiae
Y128A
about 1.5% of wild-type activity
Saccharomyces cerevisiae
Y128F
activity similar to wild-type
Saccharomyces cerevisiae
Y165A
complete loss of activity
Saccharomyces cerevisiae
Y165F
complete loss of activity
Saccharomyces cerevisiae
Y198F
about 75% of wild-type activity
Saccharomyces cerevisiae
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.12
-
3-Methylbutanal
mutant Y198F, pH 7.5, 30°C
Saccharomyces cerevisiae
0.14
-
3-Methylbutanal
wild-type, pH 7.5, 30°C
Saccharomyces cerevisiae
0.18
-
3-Methylbutanal
mutant F132A, pH 7.5, 30°C
Saccharomyces cerevisiae
0.2
-
3-Methylbutanal
mutant V162A, pH 7.5, 30°C
Saccharomyces cerevisiae
0.23
-
3-Methylbutanal
mutant Y128F, pH 7.5, 30°C
Saccharomyces cerevisiae
0.67
-
3-Methylbutanal
mutant Y128A, pH 7.5, 30°C
Saccharomyces cerevisiae
4.1
-
3-Methylbutanal
mutant Y198A, pH 7.5, 30°C
Saccharomyces cerevisiae
11.1
-
3-Methylbutanal
mutant F85A, pH 7.5, 30°C
Saccharomyces cerevisiae
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
3-methylbutanal + NAD(P)H + H+
-
737753
Saccharomyces cerevisiae
3-methylbutanol + NAD(P)+
-
-
-
r
Turnover Number [1/s] (protein specific)
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
1.4
-
3-Methylbutanal
mutant Y128A, pH 7.5, 30°C
Saccharomyces cerevisiae
5.9
-
3-Methylbutanal
mutant F85A, pH 7.5, 30°C
Saccharomyces cerevisiae
9.3
-
3-Methylbutanal
mutant Y198A, pH 7.5, 30°C
Saccharomyces cerevisiae
15.5
-
3-Methylbutanal
mutant Y198F, pH 7.5, 30°C
Saccharomyces cerevisiae
23.2
-
3-Methylbutanal
wild-type, pH 7.5, 30°C
Saccharomyces cerevisiae
38.9
-
3-Methylbutanal
mutant Y128F, pH 7.5, 30°C
Saccharomyces cerevisiae
52.6
-
3-Methylbutanal
mutant V162A, pH 7.5, 30°C
Saccharomyces cerevisiae
62.4
-
3-Methylbutanal
mutant F132A, pH 7.5, 30°C
Saccharomyces cerevisiae
KCat/KM [mM/s]
kcat/KM Value [1/mMs-1]
kcat/KM Value Maximum [1/mMs-1]
Substrate
Commentary
Organism
Structure
0.53
-
3-Methylbutanal
mutant F85A, pH 7.5, 30°C
Saccharomyces cerevisiae
2.1
-
3-Methylbutanal
mutant Y128A, pH 7.5, 30°C
Saccharomyces cerevisiae
2.3
-
3-Methylbutanal
mutant Y198A, pH 7.5, 30°C
Saccharomyces cerevisiae
126.3
-
3-Methylbutanal
mutant Y198F, pH 7.5, 30°C
Saccharomyces cerevisiae
161
-
3-Methylbutanal
wild-type, pH 7.5, 30°C
Saccharomyces cerevisiae
166.6
-
3-Methylbutanal
mutant Y128F, pH 7.5, 30°C
Saccharomyces cerevisiae
261.5
-
3-Methylbutanal
mutant V162A, pH 7.5, 30°C
Saccharomyces cerevisiae
342.7
-
3-Methylbutanal
mutant F132A, pH 7.5, 30°C
Saccharomyces cerevisiae
KCat/KM [mM/s] (protein specific)
KCat/KM Value [1/mMs-1]
KCat/KM Value Maximum [1/mMs-1]
Substrate
Commentary
Organism
Structure
0.53
-
3-Methylbutanal
mutant F85A, pH 7.5, 30°C
Saccharomyces cerevisiae
2.1
-
3-Methylbutanal
mutant Y128A, pH 7.5, 30°C
Saccharomyces cerevisiae
2.3
-
3-Methylbutanal
mutant Y198A, pH 7.5, 30°C
Saccharomyces cerevisiae
126.3
-
3-Methylbutanal
mutant Y198F, pH 7.5, 30°C
Saccharomyces cerevisiae
161
-
3-Methylbutanal
wild-type, pH 7.5, 30°C
Saccharomyces cerevisiae
166.6
-
3-Methylbutanal
mutant Y128F, pH 7.5, 30°C
Saccharomyces cerevisiae
261.5
-
3-Methylbutanal
mutant V162A, pH 7.5, 30°C
Saccharomyces cerevisiae
342.7
-
3-Methylbutanal
mutant F132A, pH 7.5, 30°C
Saccharomyces cerevisiae
Other publictions for EC 1.1.1.265
No.
1st author
Pub Med
title
organims
journal
volume
pages
year
Activating Compound
Application
Cloned(Commentary)
Crystallization (Commentary)
Engineering
General Stability
Inhibitors
KM Value [mM]
Localization
Metals/Ions
Molecular Weight [Da]
Natural Substrates/ Products (Substrates)
Organic Solvent Stability
Organism
Oxidation Stability
Posttranslational Modification
Purification (Commentary)
Reaction
Renatured (Commentary)
Source Tissue
Specific Activity [micromol/min/mg]
Storage Stability
Substrates and Products (Substrate)
Subunits
Temperature Optimum [°C]
Temperature Range [°C]
Temperature Stability [°C]
Turnover Number [1/s]
pH Optimum
pH Range
pH Stability
Cofactor
Ki Value [mM]
pI Value
IC50 Value
Activating Compound (protein specific)
Application (protein specific)
Cloned(Commentary) (protein specific)
Cofactor (protein specific)
Crystallization (Commentary) (protein specific)
Engineering (protein specific)
General Stability (protein specific)
IC50 Value (protein specific)
Inhibitors (protein specific)
Ki Value [mM] (protein specific)
KM Value [mM] (protein specific)
Localization (protein specific)
Metals/Ions (protein specific)
Molecular Weight [Da] (protein specific)
Natural Substrates/ Products (Substrates) (protein specific)
Organic Solvent Stability (protein specific)
Oxidation Stability (protein specific)
Posttranslational Modification (protein specific)
Purification (Commentary) (protein specific)
Renatured (Commentary) (protein specific)
Source Tissue (protein specific)
Specific Activity [micromol/min/mg] (protein specific)
Storage Stability (protein specific)
Substrates and Products (Substrate) (protein specific)
Subunits (protein specific)
Temperature Optimum [°C] (protein specific)
Temperature Range [°C] (protein specific)
Temperature Stability [°C] (protein specific)
Turnover Number [1/s] (protein specific)
pH Optimum (protein specific)
pH Range (protein specific)
pH Stability (protein specific)
pI Value (protein specific)
Expression
General Information
General Information (protein specific)
Expression (protein specific)
KCat/KM [mM/s]
KCat/KM [mM/s] (protein specific)
737753
Guo
Structural insights into the c ...
Saccharomyces cerevisiae
Biochim. Biophys. Acta
1844
1486-1492
2014
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1
1
11
-
-
8
-
-
-
-
-
1
-
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1
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8
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1
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1
11
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8
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-
-
-
-
-
1
-
-
-
-
8
-
-
-
-
-
-
-
-
8
8
710768
Breicha
Crystallization and preliminar ...
Saccharomyces cerevisiae
Acta Crystallogr. Sect. F
66
838-841
2010
-
-
1
1
-
-
-
-
-
-
-
-
-
2
-
-
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-
-
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1
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1
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686820
Hauser
A transcriptome analysis of is ...
Saccharomyces cerevisiae
FEMS Yeast Res.
7
84-92
2007
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-
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-
1
-
-
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-
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-
1
-
2
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-
-
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2
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2
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2
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1
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1
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2
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739760
Warringer
Involvement of yeast YOL151W/G ...
Saccharomyces cerevisiae
Yeast
23
389-398
2006
-
-
-
-
-
-
-
-
-
-
-
-
-
2
-
-
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-
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-
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1
1
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-
-
246373
Perpete
Contribution of 3-methylthiopr ...
Candida boidinii, Saccharomyces bayanus, Saccharomyces cerevisiae, Saccharomyces ludwigii
J. Agric. Food Chem.
47
2374-2378
1999
-
-
-
-
-
-
-
-
1
-
-
4
-
6
-
-
-
-
-
4
-
-
5
-
-
-
-
-
-
-
-
8
-
-
-
-
-
-
8
-
-
-
-
-
-
-
1
-
-
4
-
-
-
-
-
4
-
-
5
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
246375
Van Nedervelde
-
Purificationa nd characterizat ...
Saccharomyces cerevisiae
Proc. Congr. Eur. Brew. Conv.
26
447-454
1997
-
-
-
-
-
-
10
-
-
-
-
4
-
1
-
-
1
-
-
1
1
-
12
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
10
-
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-
4
-
-
-
1
-
1
1
-
12
-
-
-
-
-
-
-
-
-
-
-
-
-
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-
286203
Van Iersel
Purification and characterizat ...
Saccharomyces cerevisiae
Appl. Environ. Microbiol.
63
4079-4082
1997
2
1
-
-
-
-
10
19
-
-
1
2
-
2
-
-
1
-
-
1
2
-
14
1
-
-
-
17
2
-
-
2
-
-
-
2
1
-
2
-
-
-
-
10
-
19
-
-
1
2
-
-
-
1
-
1
2
-
14
1
-
-
-
17
2
-
-
-
-
-
-
-
-
-