BRENDA - Enzyme Database show

Crystal structures of homoserine dehydrogenase suggest a novel catalytic mechanism for oxidoreductases

DeLaBarre, B.; Thompson, P.R.; Wright, G.D.; Berghuis, A.M.; Nat. Struct. Biol. 7, 238-244 (2000)

Data extracted from this reference:

Crystallization (Commentary)
EC Number
Crystallization
Organism
1.1.1.3
-
Saccharomyces cerevisiae
Organism
EC Number
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
1.1.1.3
Saccharomyces cerevisiae
P31116
-
-
Substrates and Products (Substrate)
EC Number
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
1.1.1.3
L-aspartate 4-semialdehyde + NAD(P)H
-
246396
Saccharomyces cerevisiae
L-homoserine + NAD(P)+
-
246396
Saccharomyces cerevisiae
-
Subunits
EC Number
Subunits
Commentary
Organism
1.1.1.3
dimer
crystal structure
Saccharomyces cerevisiae
Cofactor
EC Number
Cofactor
Commentary
Organism
Structure
1.1.1.3
NADH
-
Saccharomyces cerevisiae
1.1.1.3
NADPH
-
Saccharomyces cerevisiae
Cofactor (protein specific)
EC Number
Cofactor
Commentary
Organism
Structure
1.1.1.3
NADH
-
Saccharomyces cerevisiae
1.1.1.3
NADPH
-
Saccharomyces cerevisiae
Crystallization (Commentary) (protein specific)
EC Number
Crystallization
Organism
1.1.1.3
-
Saccharomyces cerevisiae
Substrates and Products (Substrate) (protein specific)
EC Number
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
1.1.1.3
L-aspartate 4-semialdehyde + NAD(P)H
-
246396
Saccharomyces cerevisiae
L-homoserine + NAD(P)+
-
246396
Saccharomyces cerevisiae
-
Subunits (protein specific)
EC Number
Subunits
Commentary
Organism
1.1.1.3
dimer
crystal structure
Saccharomyces cerevisiae