BRENDA - Enzyme Database show
show all sequences of 1.1.1.203

Crystal structure of uronate dehydrogenase from Agrobacterium tumefaciens

Parkkinen, T.; Boer, H.; Jaenis, J.; Andberg, M.; Penttilae, M.; Koivula, A.; Rouvinen, J.; J. Biol. Chem. 286, 27294-27300 (2011)

Data extracted from this reference:

Cloned(Commentary)
Commentary
Organism
-
Agrobacterium tumefaciens
Crystallization (Commentary)
Crystallization
Organism
crystal structures of an apo-form, a ternary form in complex with NADH and product, and an inactive Y136A mutant in complex with NAD+. Enzyme is a homohexamer. The monomer contains a Rossmann fold, essential for nucleotide binding. The ternary complex structure reveals a product, D-galactaro-1,5-lactone, which is bound above the nicotinamide ring. This product rearranges in solution to D-galactaro-1,4-lactone
Agrobacterium tumefaciens
Engineering
Amino acid exchange
Commentary
Organism
Y136A
inactive. Crystal strucuture shows changes in the position of residues Ile74 and Ser75. This probably alters the binding of the nicotinamide end of NAD+
Agrobacterium tumefaciens
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
D-galacturonate + NAD+ + H2O
Agrobacterium tumefaciens
-
D-galactarate + NADH + H+
-
-
?
D-galacturonate + NAD+ + H2O
Agrobacterium tumefaciens C58
-
D-galactarate + NADH + H+
-
-
?
D-glucuronate + NAD+ + H2O
Agrobacterium tumefaciens
-
D-glucaric acid + NADH + H+
-
-
?
D-glucuronate + NAD+ + H2O
Agrobacterium tumefaciens C58
-
D-glucaric acid + NADH + H+
-
-
?
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Agrobacterium tumefaciens
Q7CRQ0
-
-
Agrobacterium tumefaciens C58
Q7CRQ0
-
-
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
D-galacturonate + NAD+ + H2O
-
725435
Agrobacterium tumefaciens
D-galactarate + NADH + H+
-
-
-
?
D-galacturonate + NAD+ + H2O
-
725435
Agrobacterium tumefaciens C58
D-galactarate + NADH + H+
-
-
-
?
D-glucuronate + NAD+ + H2O
-
725435
Agrobacterium tumefaciens
D-glucaric acid + NADH + H+
-
-
-
?
D-glucuronate + NAD+ + H2O
-
725435
Agrobacterium tumefaciens C58
D-glucaric acid + NADH + H+
-
-
-
?
Cofactor
Cofactor
Commentary
Organism
Structure
NAD+
-
Agrobacterium tumefaciens
Cloned(Commentary) (protein specific)
Commentary
Organism
-
Agrobacterium tumefaciens
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
NAD+
-
Agrobacterium tumefaciens
Crystallization (Commentary) (protein specific)
Crystallization
Organism
crystal structures of an apo-form, a ternary form in complex with NADH and product, and an inactive Y136A mutant in complex with NAD+. Enzyme is a homohexamer. The monomer contains a Rossmann fold, essential for nucleotide binding. The ternary complex structure reveals a product, D-galactaro-1,5-lactone, which is bound above the nicotinamide ring. This product rearranges in solution to D-galactaro-1,4-lactone
Agrobacterium tumefaciens
Engineering (protein specific)
Amino acid exchange
Commentary
Organism
Y136A
inactive. Crystal strucuture shows changes in the position of residues Ile74 and Ser75. This probably alters the binding of the nicotinamide end of NAD+
Agrobacterium tumefaciens
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
D-galacturonate + NAD+ + H2O
Agrobacterium tumefaciens
-
D-galactarate + NADH + H+
-
-
?
D-galacturonate + NAD+ + H2O
Agrobacterium tumefaciens C58
-
D-galactarate + NADH + H+
-
-
?
D-glucuronate + NAD+ + H2O
Agrobacterium tumefaciens
-
D-glucaric acid + NADH + H+
-
-
?
D-glucuronate + NAD+ + H2O
Agrobacterium tumefaciens C58
-
D-glucaric acid + NADH + H+
-
-
?
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
D-galacturonate + NAD+ + H2O
-
725435
Agrobacterium tumefaciens
D-galactarate + NADH + H+
-
-
-
?
D-galacturonate + NAD+ + H2O
-
725435
Agrobacterium tumefaciens C58
D-galactarate + NADH + H+
-
-
-
?
D-glucuronate + NAD+ + H2O
-
725435
Agrobacterium tumefaciens
D-glucaric acid + NADH + H+
-
-
-
?
D-glucuronate + NAD+ + H2O
-
725435
Agrobacterium tumefaciens C58
D-glucaric acid + NADH + H+
-
-
-
?
Other publictions for EC 1.1.1.203
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)
725435
Parkkinen
Crystal structure of uronate d ...
Agrobacterium tumefaciens, Agrobacterium tumefaciens C58
J. Biol. Chem.
286
27294-27300
2011
-
-
1
1
1
-
-
-
-
-
-
4
-
6
-
-
-
-
-
-
-
-
4
-
-
-
-
-
-
-
-
1
-
-
-
-
-
1
1
1
1
-
-
-
-
-
-
-
-
4
-
-
-
-
-
-
-
-
4
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
695552
Moon
Enzymatic assay of D-glucurona ...
Agrobacterium tumefaciens, Agrobacterium tumefaciens C58
Anal. Biochem.
392
183-185
2009
-
1
1
-
-
-
-
-
-
-
-
-
-
20
-
-
1
-
-
-
-
1
2
-
-
-
-
-
-
-
-
1
-
-
-
-
1
1
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
1
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
695783
Moon
Production of glucaric acid fr ...
Pseudomonas syringae pv. tomato
Appl. Environ. Microbiol.
75
589-595
2009
-
-
1
-
-
-
-
-
-
-
-
-
-
5
-
-
-
-
-
-
1
-
2
-
-
-
-
-
1
-
-
1
-
-
-
-
-
1
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
2
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
698607
Yoon
Cloning and characterization o ...
Agrobacterium tumefaciens, Agrobacterium tumefaciens C58, Pseudomonas putida KT2440, Pseudomonas syringae pv. tomato
J. Bacteriol.
191
1565-1573
2009
-
-
3
-
-
-
-
9
-
-
3
-
-
13
-
-
3
-
-
-
-
-
8
3
-
-
-
6
3
-
-
3
-
-
-
-
-
3
3
-
-
-
-
-
-
9
-
-
3
-
-
-
-
3
-
-
-
-
8
3
-
-
-
6
3
-
-
-
-
-
-
-
-
-
286231
Wagner
Uronic acid dehydrogenase from ...
Pseudomonas syringae
Eur. J. Biochem.
61
589-596
1976
-
-
-
-
-
1
4
3
-
-
2
2
-
2
-
-
1
-
1
1
1
2
3
1
1
-
3
2
-
-
-
1
-
-
-
-
-
-
1
-
-
1
-
4
-
3
-
-
2
2
-
-
-
1
1
1
1
2
3
1
1
-
3
2
-
-
-
-
-
-
-
-
-
-
286230
Bateman
Purification and properties of ...
Pseudomonas syringae
Arch. Biochem. Biophys.
136
97-105
1970
-
-
-
-
-
1
1
3
-
-
-
2
-
2
-
-
1
-
-
1
1
1
2
-
-
-
2
-
1
-
2
1
-
-
-
-
-
-
1
-
-
1
-
1
-
3
-
-
-
2
-
-
-
1
-
1
1
1
2
-
-
-
2
-
1
-
2
-
-
-
-
-
-
-