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Literature summary for 2.3.3.13 extracted from

  • Kumar, G.; Frantom, P.A.
    Evolutionarily distinct versions of the multidomain enzyme alpha-isopropylmalate synthase share discrete mechanisms of V-type allosteric regulation (2014), Biochemistry, 53, 4847-4856.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli Methanocaldococcus jannaschii

Inhibitors

Inhibitors Comment Organism Structure
EDTA 1 mM, 96% decrease in activity Methanocaldococcus jannaschii
L-leucine partially inhibited by L-leucine in a V-type manner Methanocaldococcus jannaschii
MgCl2 20 mM decreases activity Methanocaldococcus jannaschii
MnCl2 20 mM decreases activity Methanocaldococcus jannaschii
ZnCl2 20 mM decreases activity Methanocaldococcus jannaschii

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.07
-
acetyl-CoA pH 7.8, 37°C Methanocaldococcus jannaschii
0.09
-
3-methyl-2-oxobutanoate pH 7.8, 37°C Methanocaldococcus jannaschii

Metals/Ions

Metals/Ions Comment Organism Structure
KCl 100 mM, activity is increased 1.5fold Methanocaldococcus jannaschii
additional information the enzyme is active in the absence of exogenous monovalent or divalent metals. Addition of 1 mM EDTA results in a 96% decrease in activity, consistent with the requirement for divalent metals and suggesting that the enzyme is copurified with a divalent metal Methanocaldococcus jannaschii
NaCl 100 mM, activity is increased 1.5fold Methanocaldococcus jannaschii

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
230000
-
gel filtration Methanocaldococcus jannaschii

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
acetyl-CoA + 3-methyl-2-oxobutanoate + H2O Methanocaldococcus jannaschii the hydrolytic step is rate-determining (2S)-2-isopropylmalate + CoA
-
?
acetyl-CoA + 3-methyl-2-oxobutanoate + H2O Methanocaldococcus jannaschii DSM 2661 the hydrolytic step is rate-determining (2S)-2-isopropylmalate + CoA
-
?

Organism

Organism UniProt Comment Textmining
Methanocaldococcus jannaschii Q58595
-
-
Methanocaldococcus jannaschii DSM 2661 Q58595
-
-

Purification (Commentary)

Purification (Comment) Organism
-
Methanocaldococcus jannaschii

Storage Stability

Storage Stability Organism
-20°C, concentrated protein stored in 20% glycerol Methanocaldococcus jannaschii

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
acetyl-CoA + 3-methyl-2-oxobutanoate + H2O the hydrolytic step is rate-determining Methanocaldococcus jannaschii (2S)-2-isopropylmalate + CoA
-
?
acetyl-CoA + 3-methyl-2-oxobutanoate + H2O the hydrolytic step is rate-determining Methanocaldococcus jannaschii DSM 2661 (2S)-2-isopropylmalate + CoA
-
?

Synonyms

Synonyms Comment Organism
IPMS
-
Methanocaldococcus jannaschii
leuA
-
Methanocaldococcus jannaschii
Mj1195 locus name Methanocaldococcus jannaschii

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
assay at Methanocaldococcus jannaschii

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
90
-
the enzyme retains full activity after incubation in water for 15 min Methanocaldococcus jannaschii

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
330
-
acetyl-CoA pH 7.8, 37°C Methanocaldococcus jannaschii
330
-
3-methyl-2-oxobutanoate pH 7.8, 37°C Methanocaldococcus jannaschii
450
-
acetyl-CoA pH 7.8, 55°C Methanocaldococcus jannaschii
450
-
3-methyl-2-oxobutanoate pH 7.8, 55°C Methanocaldococcus jannaschii

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.8
-
assay at Methanocaldococcus jannaschii

Ki Value [mM]

Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
0.00016
-
L-leucine pH 7.8, 37°C Methanocaldococcus jannaschii