BRENDA - Enzyme Database show
show all sequences of 1.1.1.3

Structural basis for the catalytic mechanism of homoserine dehydrogenase

Navratna, V.; Reddy, G.; Gopal, B.; Acta Crystallogr. Sect. D 71, 1216-1225 (2015)

Data extracted from this reference:

Cloned(Commentary)
Commentary
Organism
gene hom, recombinant expression of His-tagged wild-type and mutant enzymes in Echerichia coli strain Rosetta (DE3) pLysS
Staphylococcus aureus
Crystallization (Commentary)
Crystallization
Organism
purified enzyme, crystallization at different pH values in the range of pH 6.0-8.5, X-ray diffraction structure determination and analysis at 2.1-2.2 A resolution
Staphylococcus aureus
Engineering
Amino acid exchange
Commentary
Organism
K105A
site-directed double-primer PCR mutagenesis
Staphylococcus aureus
K105R
site-directed double-primer PCR mutagenesis
Staphylococcus aureus
K205A
site-directed double-primer PCR mutagenesis
Staphylococcus aureus
Inhibitors
Inhibitors
Commentary
Organism
Structure
L-serine
allosteric inhibitor
Staphylococcus aureus
L-threonine
allosteric inhibitor
Staphylococcus aureus
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
additional information
-
additional information
kinetic profile
Staphylococcus aureus
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
L-homoserine + NADP+
Staphylococcus aureus
-
L-aspartate 4-semialdehyde + NADPH + H+
-
-
r
L-homoserine + NADP+
Staphylococcus aureus COL
-
L-aspartate 4-semialdehyde + NADPH + H+
-
-
r
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Staphylococcus aureus
A0A0H2WVX4
-
-
Staphylococcus aureus COL
A0A0H2WVX4
-
-
Purification (Commentary)
Commentary
Organism
recombinant His-tagged wild-type and mutant enzymes from Echerichia coli strain Rosetta (DE3) pLysS by nickel affinty chromatography and gel filtration
Staphylococcus aureus
Reaction
Reaction
Commentary
Organism
L-homoserine + NAD(P)+ = L-aspartate 4-semialdehyde + NAD(P)H + H+
role of conserved water molecules and a lysine residue in hydride transfer between the substrate and the cofactor. Lys105, which is located at the interface of the catalytic and cofactor-binding sites, mediates the hydride transfer step of the reaction mechanism of the enzyme. Potential reaction mechanisms for homoserine dehydrogenase, overview
Staphylococcus aureus
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
L-homoserine + NADP+
-
739791
Staphylococcus aureus
L-aspartate 4-semialdehyde + NADPH + H+
-
-
-
r
L-homoserine + NADP+
-
739791
Staphylococcus aureus COL
L-aspartate 4-semialdehyde + NADPH + H+
-
-
-
r
Subunits
Subunits
Commentary
Organism
homodimer
the enzyme is a dimer in solution as well as in the crystal. Enzyme HSD from stapylococcus aureus is an elongated molecule with three domains: a nucleotide cofactor binding domain at the N-terminus, a central catalytic domain and a C-terminal ACT domain, structure overview
Staphylococcus aureus
More
structural basis for the catalytic mechanism of homoserine dehydrogenase, overview
Staphylococcus aureus
Temperature Optimum [C]
Temperature Optimum [C]
Temperature Optimum Maximum [C]
Commentary
Organism
37
-
-
Staphylococcus aureus
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
8.5
-
the catalytic activity of the enzyme for the conversion of L-homoserine to L-aspartate 4-semialdehyde (the reverse reaction) is enhanced at basic pH
Staphylococcus aureus
Cofactor
Cofactor
Commentary
Organism
Structure
NADP+
-
Staphylococcus aureus
NADPH
-
Staphylococcus aureus
Cloned(Commentary) (protein specific)
Commentary
Organism
gene hom, recombinant expression of His-tagged wild-type and mutant enzymes in Echerichia coli strain Rosetta (DE3) pLysS
Staphylococcus aureus
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
NADP+
-
Staphylococcus aureus
NADPH
-
Staphylococcus aureus
Crystallization (Commentary) (protein specific)
Crystallization
Organism
purified enzyme, crystallization at different pH values in the range of pH 6.0-8.5, X-ray diffraction structure determination and analysis at 2.1-2.2 A resolution
Staphylococcus aureus
Engineering (protein specific)
Amino acid exchange
Commentary
Organism
K105A
site-directed double-primer PCR mutagenesis
Staphylococcus aureus
K105R
site-directed double-primer PCR mutagenesis
Staphylococcus aureus
K205A
site-directed double-primer PCR mutagenesis
Staphylococcus aureus
Inhibitors (protein specific)
Inhibitors
Commentary
Organism
Structure
L-serine
allosteric inhibitor
Staphylococcus aureus
L-threonine
allosteric inhibitor
Staphylococcus aureus
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
additional information
-
additional information
kinetic profile
Staphylococcus aureus
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
L-homoserine + NADP+
Staphylococcus aureus
-
L-aspartate 4-semialdehyde + NADPH + H+
-
-
r
L-homoserine + NADP+
Staphylococcus aureus COL
-
L-aspartate 4-semialdehyde + NADPH + H+
-
-
r
Purification (Commentary) (protein specific)
Commentary
Organism
recombinant His-tagged wild-type and mutant enzymes from Echerichia coli strain Rosetta (DE3) pLysS by nickel affinty chromatography and gel filtration
Staphylococcus aureus
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
L-homoserine + NADP+
-
739791
Staphylococcus aureus
L-aspartate 4-semialdehyde + NADPH + H+
-
-
-
r
L-homoserine + NADP+
-
739791
Staphylococcus aureus COL
L-aspartate 4-semialdehyde + NADPH + H+
-
-
-
r
Subunits (protein specific)
Subunits
Commentary
Organism
homodimer
the enzyme is a dimer in solution as well as in the crystal. Enzyme HSD from stapylococcus aureus is an elongated molecule with three domains: a nucleotide cofactor binding domain at the N-terminus, a central catalytic domain and a C-terminal ACT domain, structure overview
Staphylococcus aureus
More
structural basis for the catalytic mechanism of homoserine dehydrogenase, overview
Staphylococcus aureus
Temperature Optimum [C] (protein specific)
Temperature Optimum [C]
Temperature Optimum Maximum [C]
Commentary
Organism
37
-
-
Staphylococcus aureus
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
8.5
-
the catalytic activity of the enzyme for the conversion of L-homoserine to L-aspartate 4-semialdehyde (the reverse reaction) is enhanced at basic pH
Staphylococcus aureus
General Information
General Information
Commentary
Organism
metabolism
homoserine dehydrogenase (HSD) is an oxidoreductase in the aspartic acid pathway. The L-homoserine produced by this enzyme at the first branch point of the aspartic acid pathway is a precursor for essential amino acids such as L-threonine, L-methionine and L-isoleucine
Staphylococcus aureus
additional information
structural basis for the catalytic mechanism of homoserine dehydrogenase, the cofactor-binding site and catalytic site are docked with the cofactor NADP+ and L-homoserine, respectively, modelling, overview
Staphylococcus aureus
physiological function
the enzyme coordinates a critical branch point of the metabolic pathway that leads to the synthesis of bacterial cell-wall components such as L-lysine and m-DAP in addition to other amino acids such as L-threonine, L-methionine and L-isoleucine. The kinetic behaviour of Staphylococcus aureus HSD is not altered in the presence of plausible allosteric inhibitors such as L-threonine and L-serine
Staphylococcus aureus
General Information (protein specific)
General Information
Commentary
Organism
metabolism
homoserine dehydrogenase (HSD) is an oxidoreductase in the aspartic acid pathway. The L-homoserine produced by this enzyme at the first branch point of the aspartic acid pathway is a precursor for essential amino acids such as L-threonine, L-methionine and L-isoleucine
Staphylococcus aureus
additional information
structural basis for the catalytic mechanism of homoserine dehydrogenase, the cofactor-binding site and catalytic site are docked with the cofactor NADP+ and L-homoserine, respectively, modelling, overview
Staphylococcus aureus
physiological function
the enzyme coordinates a critical branch point of the metabolic pathway that leads to the synthesis of bacterial cell-wall components such as L-lysine and m-DAP in addition to other amino acids such as L-threonine, L-methionine and L-isoleucine. The kinetic behaviour of Staphylococcus aureus HSD is not altered in the presence of plausible allosteric inhibitors such as L-threonine and L-serine
Staphylococcus aureus
Other publictions for EC 1.1.1.3
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)
740860
Tsai
Candida albicans Hom6 is a hom ...
Candida albicans, Candida albicans SC5314 / ATCC MYA-2876
J. Microbiol. Immunol. Infect.
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863-871
2017
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2
1
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1
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1
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1
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2
2
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Corynebacterium glutamicum, Corynebacterium glutamicum IWJ001
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43
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739779
Chen
Rational design of allosteric ...
Corynebacterium glutamicum
ACS Synth. Biol.
4
126-131
2015
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739791
Navratna
Structural basis for the catal ...
Staphylococcus aureus, Staphylococcus aureus COL
Acta Crystallogr. Sect. D
71
1216-1225
2015
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3
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739972
Tomonaga
Structural insight into activa ...
Sulfurisphaera tokodaii, Sulfurisphaera tokodaii DSM 16993 / JCM 10545 / NBRC 100140 / 7
Biochem. Biophys. Rep.
3
14-17
2015
1
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1
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4
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2
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1
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741408
Hayashi
Crystal structures of a hypert ...
Pyrococcus horikoshii, Pyrococcus horikoshii ATCC 700860
Sci. Rep.
5
11674
2015
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1
1
2
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1
7
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2
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2
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7
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4
1
1
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5
1
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1
1
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5
5
740548
Zhan
Exploring the molecular basis ...
Mycobacterium leprae, Mycobacterium leprae TN
Int. J. Mol. Sci.
15
1826-1841
2014
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7
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1
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741465
Shen
Heterologous expression and ch ...
Corynebacterium pekinense, Corynebacterium pekinense AS1.299
Wei Sheng Wu Xue Bao
54
1178-1184
2014
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1
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739804
Navratna
Crystallization and preliminar ...
Staphylococcus aureus, Staphylococcus aureus COL
Acta Crystallogr. Sect. F
69
1216-1219
2013
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710978
Brautaset
Bacillus methanolicus pyruvate ...
Bacillus methanolicus, Bacillus methanolicus MGA3
Appl. Microbiol. Biotechnol.
87
951-964
2010
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1
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1
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6
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712490
Schroeder
Threonine-insensitive homoseri ...
Glycine max
J. Biol. Chem.
285
827-834
2010
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23
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12
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24
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1
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12
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24
24
688167
Yilmaz
Targeted disruption of homoser ...
Streptomyces clavuligerus, Streptomyces clavuligerus NRRL 3585
J. Ind. Microbiol. Biotechnol.
35
1-7
2008
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689647
Varisi
Lysine biosynthesis and nitrog ...
Chenopodium quinoa
Plant Physiol. Biochem.
46
11-18
2008
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688822
Park
Characteristics of methionine ...
Corynebacterium glutamicum
Metab. Eng.
9
327-336
2007
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670165
Cahyanto
Regulation of aspartokinase, a ...
Lactobacillus plantarum
Microbiology
152
105-112
2006
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662432
Curien
Identification of six novel al ...
Arabidopsis thaliana
J. Biol. Chem.
280
41178-41183
2005
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654955
Ejim
New phenolic inhibitors of yea ...
Saccharomyces cerevisiae
Bioorg. Med. Chem.
12
3825-3830
2004
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13
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13
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-
-
-
642341
Paris
Mechanism of control of Arabid ...
Arabidopsis thaliana
J. Biol. Chem.
278
5361-5366
2003
-
-
-
-
2
-
1
-
-
1
2
-
-
2
-
-
-
1
-
-
-
-
1
1
1
-
-
-
1
-
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1
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1
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-
-
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-
-
-
-
-
-
1
1
1
-
-
-
1
-
-
-
-
-
-
-
-
-
657018
Rognes
Transcriptional and biochemica ...
Arabidopsis thaliana, Saccharomyces cerevisiae
Plant Mol. Biol.
51
281-294
2003
-
-
1
-
2
-
1
-
-
1
-
2
-
6
-
-
-
1
-
4
-
-
3
-
-
-
-
-
-
-
-
3
-
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-
1
3
-
2
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1
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-
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-
4
-
-
3
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
642340
Paris
Overproduction, purification, ...
Arabidopsis thaliana
Protein Expr. Purif.
24
105-110
2002
-
-
-
-
-
-
1
5
-
1
2
-
-
3
-
-
-
1
-
-
2
1
1
2
1
-
-
-
1
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-
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1
-
5
-
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2
-
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-
-
-
2
1
1
2
1
-
-
-
1
-
-
-
-
-
-
-
-
-
654640
James
Production and characterizatio ...
Escherichia coli
Biochemistry
41
3720-3725
2002
-
-
1
-
1
-
-
4
-
-
-
1
-
2
-
-
1
1
-
-
-
-
2
-
-
-
-
4
-
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1
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1
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-
4
-
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1
-
-
-
-
2
-
-
-
-
4
-
-
-
-
-
-
-
-
-
-
246401
Jacques
Homoserine dehydrogenase from ...
Saccharomyces cerevisiae
Biochim. Biophys. Acta
1544
42-54
2001
-
-
-
-
-
-
4
-
-
-
-
1
-
3
-
-
-
-
-
-
-
-
3
-
-
-
-
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4
-
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1
-
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-
-
-
-
-
3
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
246402
Jacques
Characterization of yeast homo ...
Saccharomyces cerevisiae
Biochim. Biophys. Acta
1544
28-41
2001
-
-
1
-
1
-
-
-
-
-
-
-
-
3
-
-
1
-
-
-
1
-
2
-
-
-
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1
-
-
1
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-
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-
-
1
-
-
1
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
246396
DeLaBarre
Crystal structures of homoseri ...
Saccharomyces cerevisiae
Nat. Struct. Biol.
7
238-244
2000
-
-
-
1
-
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
1
1
-
-
-
-
-
-
-
2
-
-
-
-
-
-
2
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
246394
Morbach
-
Engineering the homoserine deh ...
Corynebacterium glutamicum
Appl. Microbiol. Biotechnol.
45
612-620
1996
-
-
-
-
1
-
2
-
-
-
-
-
-
1
-
-
-
-
-
-
1
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
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-
2
-
-
-
-
-
-
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-
-
-
-
-
1
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
246395
Pavagi
Purification and characterizat ...
Spinacia oleracea
Biochem. Mol. Biol. Int.
36
649-658
1995
1
-
-
-
-
-
7
3
-
-
2
-
-
2
-
-
1
-
-
1
-
-
2
1
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
7
-
3
-
-
2
-
-
-
-
1
-
1
-
-
2
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
246387
Wedler
Kinetic and regulatory mechani ...
Escherichia coli
J. Biol. Chem.
268
4880-4888
1993
-
-
-
-
-
-
1
4
-
-
-
1
-
1
-
-
-
-
-
-
-
-
3
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
2
-
-
-
-
1
-
4
-
-
-
1
-
-
-
-
-
-
-
-
3
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
246403
Omori
Role of serine 352 in the allo ...
Serratia marcescens
J. Bacteriol.
175
959-965
1993
-
-
-
-
-
-
1
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
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-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
246398
Hama
Inhibition of homoserine dehyd ...
Escherichia coli
J. Biochem.
109
604-608
1991
-
-
-
-
-
-
3
-
-
-
-
-
-
2
-
-
1
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
3
-
-
-
-
-
-
-
-
-
1
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
246399
Yumoto
Rapid purification and charact ...
Saccharomyces cerevisiae
Arch. Biochem. Biophys.
285
270-275
1991
-
-
-
-
-
-
2
-
-
-
2
-
-
6
-
-
1
-
1
-
1
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
2
-
-
-
-
2
-
-
-
-
1
1
-
1
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
246397
Yamaki
The mechanism of antifungal ac ...
Saccharomyces cerevisiae
Biochem. Biophys. Res. Commun.
168
837-843
1990
-
-
-
-
-
-
1
-
-
-
-
-
-
4
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
246400
Angeles
The kinetic mechanism of the b ...
Escherichia coli
Arch. Biochem. Biophys.
283
96-101
1990
-
-
-
-
-
-
2
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
246383
Krishnaswamy
Use of monoclonal antibodies f ...
Zea mays
Arch. Biochem. Biophys.
246
250-262
1986
-
-
-
-
-
-
-
-
-
-
1
-
-
2
-
-
1
-
-
1
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
1
-
1
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
246384
Krishnaswamy
Ligand-induced interconversion ...
Zea mays
Arch. Biochem. Biophys.
222
449-463
1983
-
-
-
-
-
-
1
-
-
-
-
-
-
2
-
-
1
-
-
2
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
1
-
2
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
246382
Sainis
Localisation and characterisat ...
Hordeum vulgare, Pisum sativum
Planta
152
491-496
1981
-
-
-
-
-
-
4
7
4
-
4
2
-
5
-
-
2
-
-
2
-
-
6
-
-
-
-
-
-
-
-
4
-
-
-
-
-
-
4
-
-
-
-
4
-
7
4
-
4
2
-
-
-
2
-
2
-
-
6
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
246386
Di Camelli
Comparison of sensitive and de ...
Zea mays
Plant Physiol.
65
176-183
1980
-
-
-
-
-
-
1
-
-
-
-
-
-
3
-
-
-
-
-
3
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
3
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
246388
Grego
-
Comparison of homoserine dehyd ...
Pisum sativum, Ricinus communis, Triticum aestivum
Phytochemistry
19
1619-1623
1980
-
-
-
-
-
-
3
5
-
15
5
3
-
3
-
-
3
-
-
3
3
-
8
-
-
-
-
-
-
-
-
6
-
-
-
-
-
-
6
-
-
-
-
3
-
5
-
15
5
3
-
-
-
3
-
3
3
-
8
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
246385
Walter
Isolation and characterization ...
Zea mays
J. Biol. Chem.
254
1349-1355
1979
-
-
-
-
-
-
1
4
-
-
5
-
-
2
-
-
1
-
-
1
2
1
-
2
-
-
-
-
-
-
-
1
-
-
-
-
-
-
1
-
-
-
-
1
-
4
-
-
5
-
-
-
-
1
-
1
2
1
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
246389
Epstein
Homoserine dehydrogenase of Rh ...
Rhodospirillum rubrum
Eur. J. Biochem.
82
453-461
1978
-
-
-
-
-
-
1
-
-
-
3
-
-
2
-
-
1
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
3
-
-
-
-
1
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
246390
Ogilvie
Reaction of Tris with aldehyde ...
Escherichia coli
Biochim. Biophys. Acta
445
525-536
1976
-
-
-
-
-
-
1
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
246391
Aarnes
-
Threonine-sensitive aspartate ...
Pisum sativum
Phytochemistry
13
2717-2724
1974
-
-
-
-
-
-
3
2
-
-
-
-
-
1
-
-
1
-
-
1
-
1
2
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
2
-
-
-
-
3
-
2
-
-
-
-
-
-
-
1
-
1
-
1
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
246392
Cavari
Properties of homoserine dehyd ...
Thermophilic bacterium
Biochim. Biophys. Acta
302
183-190
1973
-
-
-
-
-
-
4
1
-
5
-
-
-
2
-
-
1
-
-
-
-
-
2
-
1
1
-
-
1
1
-
2
-
-
-
-
-
-
2
-
-
-
-
4
-
1
-
5
-
-
-
-
-
1
-
-
-
-
2
-
1
1
-
-
1
1
-
-
-
-
-
-
-
-
246393
Saiki
Studies on homoserine dehydrog ...
Thermus thermophilus
J. Biochem.
74
1239-1248
1973
-
-
-
-
-
-
1
1
-
2
-
-
-
2
-
-
1
-
-
-
-
-
2
-
1
-
3
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
1
-
2
-
-
-
-
-
1
-
-
-
-
2
-
1
-
3
-
1
-
-
-
-
-
-
-
-
-