2.3.3.13: 2-isopropylmalate synthase
This is an abbreviated version!
For detailed information about 2-isopropylmalate synthase, go to the full flat file.
Word Map on EC 2.3.3.13
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2.3.3.13
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l-leucine
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4.1.3.12
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alpha-ketoisovalerate
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homocitrate
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beta-isopropylmalate
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citramalate
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methylthioalkylmalate
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alpha-ketobutyrate
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alpha-ketoisocaproate
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feedback-resistant
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acetohydroxyacid
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acetohydroxy
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accoa
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medicine
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agriculture
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drug development
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food industry
- 2.3.3.13
- l-leucine
-
4.1.3.12
- alpha-ketoisovalerate
- homocitrate
- beta-isopropylmalate
- citramalate
-
methylthioalkylmalate
- alpha-ketobutyrate
- alpha-ketoisocaproate
-
feedback-resistant
-
acetohydroxyacid
-
acetohydroxy
- accoa
- medicine
- agriculture
- drug development
- food industry
Reaction
Synonyms
2-isopropylmalate synthase 1, chloroplastic, 2-isopropylmalate synthase 2, chloroplastic, 3-hydroxy-4-methyl-3-carboxy-pentanoate 2-oxo-3-methyl-butanoate lyase (CoA-acetylating), 3-hydroxy-4-methyl-3-carboxyvalerate 2-oxo-3-methyl-butyrate lyase (CoA-acetylating), alpha-IPM synthase, Alpha-IPM synthetase, alpha-IPMS, alpha-IPMS-14CR, alpha-IPMS-2CR, Alpha-isopropylmalate synthase, alpha-isopropylmalate synthase I, alpha-isopropylmalate synthase II, alpha-isopropylmalate synthetase, alpha-isopropylmalic synthetase, BatIMS, EC 4.1.3.12, IPM synthase, IPM-synthase, IPMS, IPMS1, IPMS2, IPMS3, isopropylmalate synthase, isopropylmalate synthase 1, isopropylmalate synthetase, LEU4, LEU9, leuA, Mj1195, MtalphaIPMS, MtIPMS, NmeIPMS, Os11g04670, Os12g04440, OsIPMS1, OsIPMS2, ROL17, synthase, 2-isopropylmalate, synthase, alpha-isopropylmalate, TT_C0849
ECTree
2.3.3.13 2-isopropylmalate synthaseAdvanced search results
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results (Metals Ions
Metals Ions on EC 2.3.3.13 - 2-isopropylmalate synthase
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METALS and IONS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
Co2+
K+
Li+
Mg2+
Mn2+
Na+
NH4+
only isoform IPMS1 is coactivated by monovalent metal ions like NH4+
Rb+
Zinc
Zn2+
additional information
Co2+
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ratio kcat/Kact 0.052 per s and M. Detailed kinetic analysis
K+
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strongly dependent on the presence of monovalent cations, K+ is most effective
K+
an excess amount of 50 mM K+ is included in the standard enzymatic assays. Only isoform IPMS1 is coactivated by monovalent metal ions like K+
K+
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enzyme activity increases 1.5fold in the presence of 100 mM KCl or NaCl
K+
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the activator interacts with the catalytic TIM barrel domain, it does not induce any significant effect on the enzyme structure
K+
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enzyme requires the presence of monovalent cations, K+ is most effective
Mg2+
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and Mn2+, best activators, ratio kcat/Kact 0.014 per s and M. Detailed kinetic analysis
Mn2+
after treatment with EDTA, 4 mM Mn2+ restores about 50% of the initial activity
Mn2+
after tretment with EDTA, 4 mM Mn2+ restores about 50% of the initial activity
Mn2+
most effective activator, an excess amount 2 mM Mn2+ is included in the standard enzymatic assays
Mn2+
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and Mg2+, best activators, ratio kcat/Kact 0.034 per s and M. Detailed kinetic analysis
Na+
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enzyme activity increases 1.5fold in the presence of 100 mM KCl or NaCl
Zinc
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contains approximately 4 gatoms of zinc per dimer of 130000 Da
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
additional information
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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
additional information
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the enzyme requires a divalent metal for activity and is activated by monovalent cations
