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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

Reaction

acetyl-CoA
+
3-methyl-2-oxobutanoate
 +
H2O
=
(2S)-2-isopropylmalate
 +
CoA

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 Transferases
         2.3 Acyltransferases
             2.3.3 Acyl groups converted into alkyl groups on transfer
                2.3.3.13 2-isopropylmalate synthase

Engineering

Engineering on EC 2.3.3.13 - 2-isopropylmalate synthase

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D444A
the mutant shows increased catalytic efficiency compared to the wild type enzyme
D444R
the mutant shows increased catalytic efficiency compared to the wild type enzyme
D444Y
the mutant shows decreased catalytic efficiency compared to the wild type enzyme
D546A
-
the enzyme shows wild type activity but is not inhibited by L-leucine
D563A
-
the enzyme is more sensitive to L-leucine inhibition compared to the wild type enzyme
D563N
D564A
-
the enzyme is less sensitive to L-leucine inhibition compared to the wild type enzyme
D81A
-
the mutant shows strongly decreased activity compared to the wild type enzyme
D81E
-
the mutant shows strongly decreased activity compared to the wild type enzyme
D81E/N321I
-
the mutant shows strongly decreased activity compared to the wild type enzyme
E218A
mutant, substitution at phylogenetically conserved active site residue near the interface of the catalytic and linker domains
H167A
the mutant shows reduced activity compared to the wild type enzyme
H379A
mutant, substitution at phylogenetically conserved active site residue near the interface of the catalytic and linker domains
H540A
-
the enzyme is less sensitive to L-leucine inhibition compared to the wild type enzyme
L143A
the mutant shows reduced activity compared to the wild type enzyme
L143N
the mutant shows reduced activity compared to the wild type enzyme
M559A
-
the enzyme is less sensitive to L-leucine inhibition compared to the wild type enzyme
N250A
the mutant shows reduced activity and is able to use (3RS)-3-methyl-2-oxovalerate and 4-methyl-2-oxovalerate as substrates compared to the wild type enzyme
N321A
-
the mutant shows strongly decreased activity compared to the wild type enzyme
N321I
-
the mutant shows strongly decreased activity compared to the wild type enzyme
Q566A
-
the enzyme is more sensitive to L-leucine inhibition compared to the wild type enzyme
Q84A
-
the mutant exhibits kcat values similar to that of the L-leucine inhibited wild type enzyme
R97A
the mutant shows increased catalytic efficiency compared to the wild type enzyme
S216G
the mutant shows reduced activity and is able to use (3RS)-3-methyl-2-oxovalerate and 4-methyl-2-oxovalerate as substrates compared to the wild type enzyme
S560W
-
the mutation does not affect the activity of the enzyme, but the enzyme is less sensitive to L-leucine inhibition compared to the wild type enzyme
Y169A
the mutant shows reduced activity compared to the wild type enzyme
Y169F
mutant, substitution at phylogenetically conserved active site residue near the interface of the catalytic and linker domains
Y169H
the mutant shows reduced activity compared to the wild type enzyme
Y410F
E218A
-
mutant, substitution at phylogenetically conserved active site residue near the interface of the catalytic and linker domains
-
H379A
-
mutant, substitution at phylogenetically conserved active site residue near the interface of the catalytic and linker domains
-
Y169F
-
mutant, substitution at phylogenetically conserved active site residue near the interface of the catalytic and linker domains
-
Y410F
E365Term
mutant, truncated form of NmeIPMS, loss of the regulatory domain results in a loss of the ability to catalyse the adol reaction, although the enzyme is still able to slowly hydrolyse AcCoA
D578Y
-
release of leucine feedback inhibition and hyperproduction of isoamyl alcohol in mutant cells. Mutant shows resistance to 5,5,5-trifluoro-DL-leucine
G516S
additional information