Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 2.2.1.6 extracted from

  • Karim, M.; Shim, M.; Kim, J.; Choi, K.; Kim, J.; Choi, J.; Yoon, M.
    The catalytic role of the W573 in the mobile loop of recombinant acetohydroxyacid synthase from tobacco (2006), Bull. Korean Chem. Soc., 27, 549-555.
No PubMed abstract available
Search for more literature for 2.2.1.6

Cloned(Commentary)

Cloned (Comment) Organism
expression of wild-type and mutant enzymes in Escherichia coli strain DH5alpha Nicotiana tabacum

Protein Variants

Protein Variants Comment Organism
W573F site-directed mutagenesis, the mutant shows 69fold reduced activity compared to the wild-type enzyme, substitution of the W573 residue causes significant perturbations in the activation process and in the binding site of thiamine diphosphate Nicotiana tabacum

Inhibitors

Inhibitors Comment Organism Structure
imazapyr i.e. 2-(4-isopropyl-4-methyl-5-oxo-2-imidazolin-2-yl)nicotinic acid Nicotiana tabacum
imidazolinone
-
 Nicotiana tabacum
sulfonylurea potently inhibiting herbicide Nicotiana tabacum

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
 additional information steady-state kinetics of recombinant wild-type and mutant enzymes, cofactor binding parameters, overview Nicotiana tabacum
6.53
-
 pyruvate pH 7.5, 37°C, recombinant wild-type enzyme Nicotiana tabacum
148
-
 pyruvate pH 7.5, 37°C, recombinant mutant W573F Nicotiana tabacum

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+
-
 Nicotiana tabacum

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
pyruvate Nicotiana tabacum the enzyme catalyzes the first committed step in the biosynthesis of valine, leucine, and isoleucine 2-acetolactate + CO2
-
 ?

Organism

Organism UniProt Comment Textmining
Nicotiana tabacum
-
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant wild-type and mutant enzymes from Escherichia coli strain DH5alpha Nicotiana tabacum

Reaction

Reaction Comment Organism Reaction ID
2 pyruvate = 2-acetolactate + CO2 residue W573 is structurally important for FAD binding, the maintainance of the active site structure, and catalysis Nicotiana tabacum
a

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
pyruvate
-
 Nicotiana tabacum 2-acetolactate + CO2
-
 ?
pyruvate the enzyme catalyzes the first committed step in the biosynthesis of valine, leucine, and isoleucine Nicotiana tabacum 2-acetolactate + CO2
-
 ?

Subunits

Subunits Comment Organism
dimer the mobile loop comprising residues 567-582 on the C-terminus is involved in the binding/stabilization of the active dimer and thiamin diphosphate binding, overview Nicotiana tabacum

Synonyms

Synonyms Comment Organism
acetohydroxy acid synthase
-
 Nicotiana tabacum
AHAS
-
 Nicotiana tabacum

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
 assay at Nicotiana tabacum

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
5.4
-
 pyruvate pH 7.5, 37°C, recombinant mutant W573F Nicotiana tabacum
16.1
-
 pyruvate pH 7.5, 37°C, recombinant wild-type enzyme Nicotiana tabacum

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.5
-
 assay at Nicotiana tabacum

Cofactor

Cofactor Comment Organism Structure
FAD residues W573 is structurally important for FAD binding Nicotiana tabacum
thiamine diphosphate the mobile loop comprising residues 567-582 on the C-terminus are involved in the binding/stabilization of the active dimer and thiamin diphosphate binding, overview Nicotiana tabacum