Information on EC 2.3.3.13 - 2-isopropylmalate synthase

Word Map on EC 2.3.3.13
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Specify your search results
Select one or more organisms in this record:
Show additional data
Do not include text mining results
Include (text mining) results (more...)
Include results (AMENDA + additional results, but less precise; more...)


The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea

EC NUMBER
COMMENTARY hide
2.3.3.13
-
RECOMMENDED NAME
GeneOntology No.
2-isopropylmalate synthase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
acetyl-CoA + 3-methyl-2-oxobutanoate + H2O = (2S)-2-isopropylmalate + CoA
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
aldol condensation
condensation
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
3-methylbutanol biosynthesis (engineered)
-
-
Biosynthesis of secondary metabolites
-
-
L-leucine biosynthesis
-
-
Metabolic pathways
-
-
Pyruvate metabolism
-
-
Valine, leucine and isoleucine biosynthesis
-
-
leucine metabolism
-
-
SYSTEMATIC NAME
IUBMB Comments
acetyl-CoA:3-methyl-2-oxobutanoate C-acetyltransferase (thioester-hydrolysing, carboxymethyl-forming)
Requires K+.
CAS REGISTRY NUMBER
COMMENTARY hide
9030-98-2
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Alcaligenes viscolactis
-
-
-
Manually annotated by BRENDA team
IMS 1
SwissProt
Manually annotated by BRENDA team
IMS 2
SwissProt
Manually annotated by BRENDA team
IMS 3
SwissProt
Manually annotated by BRENDA team
No. 221
-
-
Manually annotated by BRENDA team
Bacillus sp. No. 221
No. 221
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
expressed in Arabidopsis thaliana and Escherichia coli
SwissProt
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
Chromatium sp.
strain D
-
-
Manually annotated by BRENDA team
strain D
-
-
Manually annotated by BRENDA team
strain H-1204, strain L-76
-
-
Manually annotated by BRENDA team
strain B
-
-
Manually annotated by BRENDA team
Hydrogenomonas sp.
strain H16
-
-
Manually annotated by BRENDA team
-
UniProt
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
strain 23
-
-
Manually annotated by BRENDA team
strain 23
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
strain 60615
-
-
Manually annotated by BRENDA team
strain D273-10B and S288c
-
-
Manually annotated by BRENDA team
strain SK101
-
-
Manually annotated by BRENDA team
isoform IPMS3; LA071
UniProt
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
mutant M21-10
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
metabolism
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2-oxo-3-methylbutanoate + acetyl-CoA + H2O
3-hydroxy-4-methyl-3-carboxypentanoate + CoA
show the reaction diagram
2-oxo-3-methylbutanoate + acetyl-CoA + H2O
?
show the reaction diagram
2-oxo-3-methylbutanoate + butanoyl-CoA + H2O
3-ethyl-2-hydroxy-2-isopropylsuccinic acid + CoA
show the reaction diagram
-
-
-
-
?
2-oxo-3-methylbutanoate + malonyl-CoA + H2O
2-hydroxy-3-metylbutane-11,2-tricarboxyl acid + CoA
show the reaction diagram
-
-
-
-
?
2-oxo-3-methylbutanoate + propanoyl-CoA + H2O
2-hydroxy-2-isopropyl-3-methylsuccinic acid + CoA
show the reaction diagram
2-oxo-3-methylbutanoate + valeryl-CoA + H2O
2-hydroxy-2-isopropyl-3-propylsuccinic acid + CoA
show the reaction diagram
-
-
-
-
?
2-oxo-3-methylbutanoyl-methylester + H2O
3-hydroxy-3-(methoxycarbonyl)-4-methylpentanoic acid + CoA
show the reaction diagram
-
-
-
-
?
2-oxo-butanoate + acetyl-CoA + H2O
2-ethyl-2-hydroxysuccinic acid + CoA
show the reaction diagram
2-oxo-n-pentanoate + acetyl-CoA + H2O
2-hydroxy-2-propylsuccinic acid + CoA
show the reaction diagram
2-oxobutyrate + acetyl-CoA + H2O
?
show the reaction diagram
-
-
-
?
2-oxovalerate + acetyl-CoA + H2O
?
show the reaction diagram
3-fluoropyruvate + acetyl-CoA + H2O
?
show the reaction diagram
-
-
-
?
3-methyl-2-oxopentanoate + acetyl-CoA + H2O
?
show the reaction diagram
-
-
-
?
4-methylthio-2-oxopentanoate + acetyl-CoA + H2O
? + CoA
show the reaction diagram
-
at very low rate, reaction is involved in glucosinolate chain elongation
-
?
acetyl-CoA + 2-oxobutyrate + H2O
?
show the reaction diagram
-
weak substrate
-
-
?
acetyl-CoA + 2-oxoisovalerate + H2O
?
show the reaction diagram
acetyl-CoA + 2-oxovalerate + H2O
?
show the reaction diagram
-
weak substrate
-
-
?
acetyl-CoA + 3-methyl-2-oxobutanoate + H2O
(2S)-2-isopropylmalate + CoA
show the reaction diagram
acetyl-CoA + 3-methyl-2-oxobutyrate + H2O
?
show the reaction diagram
-
-
-
?
acetyl-CoA + 3-methyl-2-oxoisovalerate + H2O
?
show the reaction diagram
-
-
-
?
acetyl-CoA + 3-methyl-2-oxovalerate + H2O
?
show the reaction diagram
-
-
-
?
acetyl-CoA + 4-methylthio-2-oxobutyrate + H2O
?
show the reaction diagram
acetyl-CoA + alpha-ketoisovalerate + H2O
alpha-isopropylmalate + CoA
show the reaction diagram
acetyl-CoA + H2O
acetate + CoA
show the reaction diagram
-
-
-
-
?
acetyl-CoA + pyruvate + H2O
?
show the reaction diagram
-
weak substrate
-
-
?
alpha-ketoisovalerate + acetyl-CoA + H2O
alpha-isopropylmalate + CoA
show the reaction diagram
-
-
-
?
alpha-ketoisovalerate + H2O + acetyl-CoA
? + CoA
show the reaction diagram
-
-
-
?
alpha-ketoisovaleric acid + H2O + acetyl-CoA
? + CoA
show the reaction diagram
crotonyl-CoA + H2O
crotonate + CoA
show the reaction diagram
-
-
-
-
?
propionyl-CoA + H2O
propanoate + CoA
show the reaction diagram
-
-
-
-
?
pyruvate + acetyl-CoA + H2O
2-hydroxy-2-methylsuccinic acid + CoA
show the reaction diagram
pyruvate + acetyl-CoA + H2O
?
show the reaction diagram
-
-
-
?
additional information
?
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
2-oxo-3-methylbutanoate + acetyl-CoA + H2O
?
show the reaction diagram
acetyl-CoA + 3-methyl-2-oxobutanoate + H2O
(2S)-2-isopropylmalate + CoA
show the reaction diagram
acetyl-CoA + alpha-ketoisovalerate + H2O
alpha-isopropylmalate + CoA
show the reaction diagram
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
KCl
100 mM, activity is increased 1.5fold
NaCl
100 mM, activity is increased 1.5fold
NH4+
only isoform IPMS1 is coactivated by monovalent metal ions like NH4+
additional information
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
(S)-alpha-hydroxyisovalerate
-
-
2-Oxo-isohexanoate
2-Oxopentanoate
-
competitive
3,3-dibromopyruvate
-
-
3-Bromopyruvate
-
-
5',5',5'-trifluoroleucine
Br-
-
above 0.02 M
Ca2+
-
50% inhibition at 0.205 mM
D-leucine amide
-
weak
DL-azaleucine
-
10 mM, at pH 6.5
DL-fluoroleucine
-
at pH 7.5
F-
-
above 0.02 M
isopropylmalate
-
competitive against both 2-oxo-3-methylbutanoate and acetyl-CoA
Isovalerate
-
moderate
K+
-
at high concentrations, stimulation at lower concentrations
K2SO4
-
250 mM K2SO4, pH 7.5, 20% inhibition
KCl
-
400 mM KCl, pH 8.2, 20% inhibition
L-2-Hydroxyisopentanoate
-
-
L-isoleucine
L-leucine
L-norleucine
L-norvaline
L-Phe
-
10 mM, at pH 6.5
L-Val
-
10 mM, at pH 6.5
Leu
inhibition of both enzymes reaches a maximum of 30% to 35% around 1 mM Leu; inhibition of both enzymes reaches a maximum of 30% to 35% around 1 mM Leu
leucine
MgCl2
20 mM decreases activity
Mn2+
-
inhibitory at 20 mM
MnCl2
20 mM decreases activity
ZnCl2
20 mM decreases activity
additional information
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
-
the addition of 5 mM valine plus isoleucine with and without 5 mM threonine caused a 4-6.6fold increase in the formation of active enzyme
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0017 - 0.57
2-oxo-3-methylbutanoate
5
2-oxo-3-methylbutanoyl-methylester
-
with acetyl-CoA as cosubstrate
0.86 - 2.1
2-oxo-butanoate
0.4 - 0.41
2-oxo-n-pentanoate
0.57 - 1.8
2-oxobutanoate
0.143 - 0.215
2-oxoisovalerate
0.3
3-Fluoropyruvate
-
pH 7.5, 25C
0.005 - 0.09
3-methyl-2-oxobutanoate
0.027
3-methyl-2-oxopentanoate
-
pH 7.5, 25C
0.734
4-methylthio-2-oxobutyrate
isoform IPMS3, pH and temperature not specified in the publication
0.0011 - 0.697
acetyl-CoA
3.3
alpha-Ketobutyrate
-
pH 7.5, 25C
0.0005 - 5.4
alpha-ketoisovalerate
0.035 - 0.261
alpha-ketoisovaleric acid
0.4
Butanoyl-CoA
-
-
0.05 - 0.95
crotonyl-CoA
0.5
malonyl-CoA
-
-
0.9
pentanoyl-CoA
-
-
0.1
propanoyl-CoA
-
-
0.22
propionyl-CoA
-
hydrolysis, absence of MgCl2, pH 7.4, 25C
0.2 - 10
pyruvate
additional information
additional information
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.77 - 13
2-oxo-3-methylbutanoate
10.7
2-oxo-butanoate
Mycobacterium tuberculosis
-
pH 7.4, 25C
7
2-oxo-n-pentanoate
Mycobacterium tuberculosis
-
pH 7.4, 25C
0.49 - 1.08
2-oxoisovalerate
105
3-Fluoropyruvate
Neisseria meningitidis
-
pH 7.5, 25C
3.1 - 450
3-methyl-2-oxobutanoate
0.28
3-methyl-2-oxopentanoate
Neisseria meningitidis
-
pH 7.5, 25C
0.12
4-methylthio-2-oxobutyrate
Solanum lycopersicum
K4C627, K4CJ56
isoform IPMS3, pH and temperature not specified in the publication
0.03 - 450
acetyl-CoA
1.36
alpha-Ketobutyrate
Neisseria meningitidis
-
pH 7.5, 25C
0.022 - 4.75
alpha-ketoisovalerate
0.52 - 1.17
alpha-ketoisovaleric acid
0.04 - 0.05
crotonyl-CoA
0.04
propionyl-CoA
Mycobacterium tuberculosis
-
hydrolysis, absence of MgCl2, pH 7.4, 25C
1.5 - 6.1
pyruvate
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2.3 - 7.5
2-oxoisovalerate
758
210 - 900
3-methyl-2-oxobutanoate
829
0.16
4-methylthio-2-oxobutyrate
Solanum lycopersicum
K4C627, K4CJ56
isoform IPMS3, pH and temperature not specified in the publication
20014
27 - 210
acetyl-CoA
29
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2.5
(S)-alpha-hydroxyisovalerate
-
pH 7.5, 25C
0.1 - 0.2
2-Oxo-isohexanoate
0.03
3,3-dibromopyruvate
-
pH 7.5, 25C
0.06
3-Bromopyruvate
-
pH 7.5, 25C
0.0025
Ca2+
-
pH 7.5, 25C
0.07
CoA
0.09
desulfo-CoA
-
with respect to acetyl-CoA
0.5 - 4
isopropylmalate
230
K+
-
at high concentration
0.00016 - 0.16
L-leucine
0.001 - 20
leucine
0.00037
Zn2+
-
pH 7.5, 25C
additional information
leucine
-
Ki with and without Zn2+ or Mn2+
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.03
L-leucine
Saccharomyces cerevisiae
-
at pH 7.5 and 30C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6 - 9.5
-
pH 6.0: about 50% of maximal activity, pH 9.5: about 80% of maximal activity
7.1 - 10
-
pH 7.1: about 50% of maximal activity, pH 10.0: about 80% of maximal activity
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37 - 50
-
almost full activity
50
isoform IPMS2
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
20 - 60
-
20C: about 50% of maximal activity, 60C: about 40% of maximal activity
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
additional information
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
PDB
SCOP
CATH
ORGANISM
UNIPROT
Cytophaga hutchinsonii (strain ATCC 33406 / NCIMB 9469)
Leptospira biflexa serovar Patoc (strain Patoc 1 / ATCC 23582 / Paris)
Leptospira biflexa serovar Patoc (strain Patoc 1 / ATCC 23582 / Paris)
Leptospira interrogans serogroup Icterohaemorrhagiae serovar Lai (strain 56601)
Leptospira interrogans serogroup Icterohaemorrhagiae serovar Lai (strain 56601)
Leptospira interrogans serogroup Icterohaemorrhagiae serovar Lai (strain 56601)
Listeria monocytogenes serotype 4b (strain F2365)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Neisseria meningitidis serogroup B (strain MC58)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
39930
-
E365Term mutant, theoretical
40000
-
E365Term mutant, determined by SDS-PAGE
50000
-
x * 50000, SDS-PAGE, ultracentrifugation of the enzyme denatured in 6 M guanidine hydrochloride and 0.1 M 2-mercaptoethanol
56000
-
wild-type enzyme, determined by SDS-PAGE
56030
-
wild-type enzyme, theoretical
60000
-
2 * 60000, SDS-PAGE
62300
2 * 62300, calculated from nucleotide sequence
63100
2 * 63100, calculated, isoform IPMS1 with His-tag
64100
4 * 64100, calculated from nucleotide sequence; 4 * 64100, calculated, isoform IPMS2 with His-tag
67000
-
2 * 67000, SDS-PAGE
68416
-
x * 68416, isoenzyme I, calculation from nucleotide sequence
72000
-
2 * 72000, SDS-PAGE
74000
-
alpha-IPMS-2CR, determined by SDS-PAGE
80000
-
2 * 80000, SDS-PAGE
99000
-
alpha-IPMS-14CR, determined by SDS-PAGE
100000
-
in presence of Leu, gel filtration
114500
-
in absence of Leu, gel filtration
121000
-
in absence of Leu, gel filtration
124000
gel filtration; gel filtration, isoform IPMS1
127000
-
sedimentation equilibrium centrifugation
130000
-
cytoplasmic form, gel filtration
137000
-
in presence of substrate, gel filtration
171000
-
gel filtration
280000
gel filtration; gel filtration, isoform IPMS2
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homodimer
tetramer
4 * 64100, calculated from nucleotide sequence; 4 * 64100, calculated, isoform IPMS2 with His-tag
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
hanging drop vapor diffusion method, using 0.1 M Tris-HCl (pH 8.5), 0.8 mM sodium formate, and 30% (w/v) PEG 2000 monomethyl ether
sitting drop vapor diffusion method
-
truncated protein LeuA425, sitting drop vapor diffusion method, using 24% (w/v) PEG 3350 and 275 mM lithium nitrate
-
truncated protein E365Term, sitting drop vapor diffusion method, using 0.2 M magnesium acetate and 18% (w/v) mPEG 3350
-
comparison of wild-type and mutant D578Y structures by homology modelling. D578 is important for leucine feedback inhibition
-
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4 - 7
-
stability of the mutated alpha-IPMS is similar to that of the native alpha-IPMS in that keeping the enzyme at pH 7.5 is better than at pH 4.0
686811
4
-
enzyme inactive
636535
7.2 - 8.2
9
-
3 h, about 50% loss of activity
636516
9.5
-
3 h, about 30% of maximal activity
636516
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
45
the stability of isoform IPMS2 isremarkably decreased when the temperature exceeds 45C and is higher than that of isoform IPMS1 at 37C
49
-
7 min, 90% loss of activity in absence of Leu, about 50% loss of activity after 15 min in presence of 0.2 mM Leu
50
-
pH 6.9, 5 min, 80% loss of activity, 1 mM Leu provides significant but incomplete protection
60
-
5 min, in absence of substrates irreversible denaturation
65
-
5 min, in presence of 2-oxo-3-methylbutanoate and acetyl-CoA, stable
additional information
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
partial deletion of the regulatory domain of isoform IPMS1 results in a loss of about 50% of the catalytic activity
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-18C, 50 mM potassium phosphate, pH 7.2, loss of activity after 3 months
-
-20C, concentrated protein stored in 20% glycerol
-20C, phosphate leucine buffer, little loss of activity
-
0C, more than 80% loss of activity after 2 d
-
22C, in presence of 0.05% sodium azide, 8% loss of activity after 3 months
-
30C, pH 7.5, stable for more than 10 days
-
freezing at -20C and thawing, about 10% loss of activity. Storage at -20C, 100 mM potassium phosphate, 0.2 mM 2-oxo-3-methylbutanoate, pH 7.5 or pH 8.0, no further loss of activity after 5 months
-
in an icebox, pH 7.5-8.5, 30% loss of activity after 48 h
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
HisTrap column chromatography
-
HiTrap affinity column chromatography and gel Sephacryl 26/60 filtration
-
Ni-NTA column chromatography
Ni-NTA column chromatography; Ni-NTA column chromatography
Ni2+ HisTrap column chromatography
-
on a nickel-NTA, a Mono-Q and a Phenyl Sepharose column
-
Q sepharose column chromatography
-
recombinant enzyme
-
recombinant enzyme using His-tag
-
TALON affinity resin column chromatography
-
Talon metal affinity resin column chromatography and Sephacryl 200 gel filtration
using Ni-NTA resin
-
using Talon Superflow Metal Affinity resin, the His-tag is removed by TEV protease, anion exchange chromatography on a SourceQ column is applied
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
construction of a Leu4'-'lacZ fusion. The Leu4 gene encodes 2 forms: a short cytoplasmic form and a long form that is targeted to the mitochondria
-
construction of three knock-out mutants, two carrying a deletion in YOR108w or in Leu4 ORF, and one carrying both the deletions
-
expressed as His-tag fusion protein in Escherichia coli BL21(DE3)
-
expressed in a Schizosaccharomyces pombe leu3DELTA deletion strain
-
expressed in Escherichia coli BL21 Rosetta cells
expressed in Escherichia coli BL21 Rosetta cells; expressed in Escherichia coli BL21 Rosetta cells
expressed in Escherichia coli BL21(DE3) cells
expressed in Escherichia coli BL21(DE3) Star cells
-
expressed in Escherichia coli BL21(DE3)pLysS cells
expression in Escherichia coli
expression in Escherichia coli and Bacillus subtilis
-
expression in Escherichia coli; expression in Escherichia coli
H37Rv leuA gene with and without the tandem repeats is cloned by PCR and expressed in an Escherichia coli host. The 57-bp tandem repeats located in the leuA gene code for the alpha-isopropylmalate synthase. Deletion of the repeats has no detectable effect on leuA expression level or the general properties of the enzyme product
-
into the vector pET-151 for expression in Escherichia coli BL21DE3 Star cells
-
into the vector pET28a for expression in Escherichia coli BL21DE3 pLysS cells
-
the coding sequences of alpha-IPMS-2CR and alpha-IPMS-14CR are cloned into the vector pET15b for expression in Escherichia coli BL21DE3 cells
-
truncated protein E365Term is expressed in Escherichia coli BL21(DE3) Star cells and in Escherichia coli strain BW25113 lacking the alpha-isopropylmalate synthase gene
-
truncated protein LeuA425 is expressed in Escherichia coli Rosetta 2 cells and in Escherichia coli strain BW25113 lacking the alpha-isopropylmalate synthase gene
-