BRENDA - Enzyme Database show
show all sequences of 1.20.1.1

Crystal structures of phosphite dehydrogenase provide insights into nicotinamide cofactor regeneration

Zou, Y.; Zhang, H.; Brunzelle, J.S.; Johannes, T.W.; Woodyer, R.; Hung, J.E.; Nair, N.; van der Donk, W.A.; Zhao, H.; Nair, S.K.; Biochemistry 51, 4263-4270 (2012)

Data extracted from this reference:

Cloned(Commentary)
Commentary
Organism
expression in Escherichia coli
Pseudomonas stutzeri
Crystallization (Commentary)
Crystallization
Organism
mutant D13E/M26I/V71I/E130K/Q132R/Q137R/I150F/E175A/Q215L/R275Q/L276Q/I313L/V315A/A319E/A325V/E332N/C336D, to 2.3 A resolution. The TS-PTDH monomer may be divided into a large and a small domain, separated by a flexible hinge region. The NAD+ cofactor is housed at the junction between the two domains, where residues from the large subunit engage in interactions with the ligand. In the cocrystal structure with NAD+ and inhibitor sulfite, the sulfite anion is situated proximal to the nicotinamide of the cofactor, where it is engaged through interactions with the side chains of Arg237, His292, and the backbone amides of Lys76 and Gly77
Pseudomonas stutzeri
Engineering
Amino acid exchange
Commentary
Organism
D13E/M26I/V71I/E130K/Q132R/Q137R/I150F/E175A/Q215L/R275Q/L276Q/I313L/V315A/A319E/A325V/E332N/C336D
thermostable mutant TS-PTDH which contains 12 mutations that result in considerably increased thermostability with minimal change in activity, and four additional mutations that increase its activity. Mutation E175A leads to relaxation of cofactor specificity
Pseudomonas stutzeri
Inhibitors
Inhibitors
Commentary
Organism
Structure
sulfite
competitive, cocrystal structure
Pseudomonas stutzeri
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Pseudomonas stutzeri
O69054
-
-
Cloned(Commentary) (protein specific)
Commentary
Organism
expression in Escherichia coli
Pseudomonas stutzeri
Crystallization (Commentary) (protein specific)
Crystallization
Organism
mutant D13E/M26I/V71I/E130K/Q132R/Q137R/I150F/E175A/Q215L/R275Q/L276Q/I313L/V315A/A319E/A325V/E332N/C336D, to 2.3 A resolution. The TS-PTDH monomer may be divided into a large and a small domain, separated by a flexible hinge region. The NAD+ cofactor is housed at the junction between the two domains, where residues from the large subunit engage in interactions with the ligand. In the cocrystal structure with NAD+ and inhibitor sulfite, the sulfite anion is situated proximal to the nicotinamide of the cofactor, where it is engaged through interactions with the side chains of Arg237, His292, and the backbone amides of Lys76 and Gly77
Pseudomonas stutzeri
Engineering (protein specific)
Amino acid exchange
Commentary
Organism
D13E/M26I/V71I/E130K/Q132R/Q137R/I150F/E175A/Q215L/R275Q/L276Q/I313L/V315A/A319E/A325V/E332N/C336D
thermostable mutant TS-PTDH which contains 12 mutations that result in considerably increased thermostability with minimal change in activity, and four additional mutations that increase its activity. Mutation E175A leads to relaxation of cofactor specificity
Pseudomonas stutzeri
Inhibitors (protein specific)
Inhibitors
Commentary
Organism
Structure
sulfite
competitive, cocrystal structure
Pseudomonas stutzeri
Other publictions for EC 1.20.1.1
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)
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1
-
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-
-
-
-
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-
746256
Hung
Chemical rescue and inhibitio ...
Pseudomonas stutzeri, Pseudomonas stutzeri WM88
PLoS ONE
9
e87134
2014
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-
-
1
2
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1
3
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2
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4
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1
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1
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1
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2
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726694
Liu
Cloning, expression, and chara ...
Pseudomonas sp., Pseudomonas sp. K
Appl. Biochem. Biotechnol.
166
1301-1313
2012
-
-
1
1
-
-
4
2
-
3
2
-
-
6
-
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1
-
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1
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2
1
1
2
3
-
1
2
1
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1
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1
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4
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2
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3
2
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1
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1
-
2
1
1
2
3
-
1
2
1
-
-
-
-
-
-
-
726981
Hung
Investigation of the role of A ...
Cupriavidus metallidurans, Cupriavidus metallidurans CH34, Methylorubrum extorquens, Methylorubrum extorquens ATCC 14718 / DSM 1338 / JCM 2805 / NCIMB 9133 / AM1, Nostoc punctiforme, Pseudomonas stutzeri
Biochemistry
51
4254-4262
2012
-
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4
-
28
-
4
22
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25
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6
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11
-
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3
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4
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28
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4
3
22
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6
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11
-
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7
7
726982
Zou
Crystal structures of phosphit ...
Pseudomonas stutzeri
Biochemistry
51
4263-4270
2012
-
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1
1
1
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1
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1
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1
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1
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-
728004
Hirota
Isolation and characterization ...
Pseudomonas stutzeri, Pseudomonas stutzeri WM88, Ralstonia sp., Ralstonia sp. 4506
J. Biosci. Bioeng.
113
445-450
2012
-
-
2
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-
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7
8
1
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11
-
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4
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2
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2
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2
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7
-
8
1
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4
-
2
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2
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-
691424
McLachlan
Further improvement of phosphi ...
Pseudomonas stutzeri
Biotechnol. Bioeng.
99
268-274
2008
-
1
1
-
33
-
-
10
-
-
-
-
-
1
-
-
1
-
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-
-
1
1
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4
-
-
-
1
-
-
-
-
1
1
1
-
33
-
-
-
-
10
-
-
-
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-
-
-
1
-
-
-
1
1
-
-
-
-
4
-
-
-
-
-
-
-
-
-
-
672712
Johannes
Efficient regeneration of NADP ...
Pseudomonas stutzeri
Biotechnol. Bioeng.
96
18-26
2007
-
1
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-
1
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4
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690884
Fogle
Pre-steady-state studies of ph ...
Pseudomonas stutzeri, Pseudomonas stutzeri WW88
Biochemistry
46
13101-13108
2007
-
1
1
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6
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1
8
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2
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1
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2
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9
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1
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1
1
1
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6
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1
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8
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1
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2
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9
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673144
Woodyer
Optimizing a biocatalyst for i ...
Pseudomonas stutzeri
Comb. Chem. High Throughput Screen.
9
237-245
2006
-
1
-
-
7
-
-
25
-
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2
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2
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12
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1
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7
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25
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2
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12
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658120
Woodyer
Site-directed mutagenesis of a ...
Pseudomonas stutzeri, Pseudomonas stutzeri WM 88
Biochemistry
44
4765-4774
2005
-
-
1
-
12
-
2
13
-
-
2
2
-
2
-
-
1
-
-
-
-
-
4
1
-
-
-
7
1
1
-
1
-
-
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-
-
1
1
-
12
-
-
2
-
13
-
-
2
2
-
-
-
1
-
-
-
-
4
1
-
-
-
7
1
1
-
-
-
-
-
-
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-
658126
Relyea
Inhibition and pH dependence o ...
Pseudomonas stutzeri
Biochemistry
44
6640-6649
2005
-
-
-
-
-
-
1
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-
-
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1
-
1
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3
-
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1
1
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1
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1
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1
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1
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3
-
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1
1
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658259
Relyea
Mechanism and applications of ...
Alcaligenes faecalis, Pseudomonas stutzeri, Pseudomonas stutzeri WM88
Bioorg. Chem.
33
171-189
2005
-
1
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6
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2
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3
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5
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1
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10
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1
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1
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6
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2
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3
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10
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1
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1
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671425
Johannes
Directed evolution of a thermo ...
Pseudomonas stutzeri
Appl. Environ. Microbiol.
71
5728-5734
2005
-
1
-
-
17
-
-
33
-
-
-
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3
-
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1
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2
12
-
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1
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17
-
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33
-
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1
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2
12
-
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673526
Woodyer
Mechanistic investigation of a ...
Pseudomonas stutzeri
FEBS J.
272
3816-3827
2005
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1
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1
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657956
Woodyer
Relaxing the nicotinamide cofa ...
Pseudomonas stutzeri
Biochemistry
42
11604-11614
2003
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1
1
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3
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8
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1
1
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2
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1
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1
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7
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8
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1
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7
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3
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287853
Costas
Purification and characterizat ...
Pseudomonas stutzeri
J. Biol. Chem.
276
17429-17436
2001
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1
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9
2
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1
1
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3
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1
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1
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9
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1
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4
1
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1
1
1
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287854
Vrtis
Phosphite dehydrogenase: An un ...
Pseudomonas stutzeri
J. Am. Chem. Soc.
123
2672-2673
2001
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1
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