Information on EC 2.3.1.182 - (R)-citramalate synthase

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

EC NUMBER
COMMENTARY hide
2.3.1.182
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RECOMMENDED NAME
GeneOntology No.
(R)-citramalate synthase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
acetyl-CoA + pyruvate + H2O = CoA + (2R)-2-hydroxy-2-methylbutanedioate
show the reaction diagram
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
aldol condensation
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condensation
elimination
enolization
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
C5-Branched dibasic acid metabolism
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L-isoleucine biosynthesis II
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Metabolic pathways
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Valine, leucine and isoleucine biosynthesis
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isoleucine metabolism
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Cyanothece sp.
an aerobic unicellular marine cyanobacterium, gene cimA
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Manually annotated by BRENDA team
2-isopropylmalate synthase
UniProt
Manually annotated by BRENDA team
strain BW25113, JCL16, KS145, SA405, SA408
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Manually annotated by BRENDA team
strain X514
UniProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
metabolism
physiological function
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(2S)-2-hydroxy-2-methylbutanedioate
acetate + pyruvate
show the reaction diagram
acetyl-CoA + 2-oxobutyrate + H2O
?
show the reaction diagram
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-
-
-
?
acetyl-CoA + 2-oxoisovalerate + H2O
?
show the reaction diagram
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-
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?
acetyl-CoA + glyoxylate + H2O
?
show the reaction diagram
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?
acetyl-CoA + pyruvate
(2S)-2-hydroxy-2-methylbutanedioate + CoA
show the reaction diagram
acetyl-CoA + pyruvate
(3S)-citramalyl-CoA
show the reaction diagram
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the enzyme is strictly specific for pyruvate as keto acid substrate
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?
acetyl-CoA + pyruvate
CoA + (R)-citramalate
show the reaction diagram
acetyl-CoA + pyruvate + H2O
CoA + (2R)-2-hydroxy-2-methyl-butanedioate
show the reaction diagram
acetyl-CoA + pyruvate + H2O
CoA + (2R)-2-hydroxy-2-methylbutanedioate
show the reaction diagram
acetyl-CoA + pyruvate + H2O
CoA + (2S)-2-hydroxy-2-methylbutanedioate
show the reaction diagram
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r
acetyl-CoA + pyruvate + H2O
CoA + (R)-citramalate
show the reaction diagram
pyruvate + acetyl-CoA + H2O
(2R)-2-hydroxy-2-methylbutanedioate + CoA
show the reaction diagram
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?
additional information
?
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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
(2S)-2-hydroxy-2-methylbutanedioate
acetate + pyruvate
show the reaction diagram
acetyl-CoA + pyruvate
CoA + (R)-citramalate
show the reaction diagram
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the enzyme is involved in the threonine-independent biosynthesis of isoleucine via an alternative beta-methyl-D-malate pathway, the expression of cimA is transcriptionally regulated by isoleucine
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?
acetyl-CoA + pyruvate + H2O
CoA + (2R)-2-hydroxy-2-methylbutanedioate
show the reaction diagram
acetyl-CoA + pyruvate + H2O
CoA + (2S)-2-hydroxy-2-methylbutanedioate
show the reaction diagram
Q74C76
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r
pyruvate + acetyl-CoA + H2O
(2R)-2-hydroxy-2-methylbutanedioate + CoA
show the reaction diagram
B0K6M2
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
acetyl-CoA
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Ca2+
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; enzymatic activity of LiCMS in the absence and presence of different metal ions. Ca2+ is an activator
Co2+
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; enzymatic activity of LiCMS in the absence and presence of different metal ions. Co2+ is an activator
Cu2+
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enzymatic activity of LiCMS in the absence and presence of different metal ions. Cu2+ is an inhibitor
K+
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; enzymatic activity of LiCMS in the absence and presence of different metal ions. Co-activation by K+ in the presence of Mn2+
NH4+
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; can act as a co-activator in the presence of Mn2+
Ni2+
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; enzymatic activity of LiCMS in the absence and presence of different metal ions. Ni2+ is an activator
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
isoleucine
leucine
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; inhibits only the mutants Y454A and V468A
additional information
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mutant I458A is not inhibited by isoleucine, leucine does not inhibit the wild-type and the mutants H400A/H408A, Y430L, L451V, I458A, D431A, T464A, P493A, and Q495A
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.465 - 12.61
2-oxobutyrate
0.098 - 52.85
2-oxoisovalerate
0.105 - 8.921
acetyl-CoA
1.023 - 10.6
glyoxylate
0.04 - 15.53
pyruvate
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.005 - 0.62
2-oxobutyrate
0.018 - 0.062
2-oxoisovalerate
0.017 - 11.1
acetyl-CoA
0.005 - 0.6
glyoxylate
0.12 - 9.3
pyruvate
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.74 - 9.2
acetyl-CoA
29
1.5 - 150
pyruvate
31
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.009 - 1.092
isoleucine
0.075 - 1.302
leucine
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.041 - 5.073
isoleucine
0.343 - 7.786
leucine
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.0004
strain DLCR6, cimA::Gmr; strain DLCR7, tdcB::Knr cimA::Gmr
0.0051
strain DLCR5, tdcB::Knr
0.0074
strain DL1, wild type
0.016
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pyruvate consumption measured, Rhodospirillum rubrum cells grown in medium with acetate and NaHCO3
0.017
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pyruvate consumption measured, Rhodospirillum rubrum cells grown in medium with malate
0.027
production of CoA measured at 60°C, pH 7.5
0.032
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CoA formation measured, Rhodospirillum rubrum cells grown in medium with malate
0.058
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CoA formation measured, Rhodospirillum rubrum cells grown in medium with acetate and NaHCO3
0.174
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crude extract of Escherichia coli recombinantly expressing CimA
0.2
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in the absence of metal ions; without metals
0.4
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in the presence of K+; with K+
1.1
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in the presence of Ni2+; with Ni2+
1.2
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in the presence of Mg2+; with Mg2+
2.2
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in the presence of Ca2+; with Ca2+
2.53
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purified recombinant His6-tagged enzyme
2.87
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purified recombinant enzyme
6.1
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in the presence of Mn2+ and Li+; with Li+
6.2
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in the presence of Mn2+; with Mn2+
6.5
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in the presence of Mn2+ and Na+; with Na+
7.1
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in the presence of Mn2+; with Mn2+
9
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in the presence of Mn2+ and NH4+; with NH4+
9.4
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in the presence of Mn2+ and K+; with K+
additional information
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specific activity for Zn2+ -0.04 micromol/min/mg and -0.13 micromol/min/mg for Cu2+
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.7
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activity assay; enzymatic activity assay
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30 - 70
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; directed evolution of CimA enhances the specific activity over a wide temperature range
additional information
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temperature profile, overview
PDB
SCOP
CATH
ORGANISM
UNIPROT
Leptospira interrogans serogroup Icterohaemorrhagiae serovar Lai (strain 56601)
Leptospira interrogans serogroup Icterohaemorrhagiae serovar Lai (strain 56601)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
14000
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corresponds to the C-terminal regulatory domain of LiCMS, SDS-PAGE
33000
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corresponds to the N-terminal catalytic domain of LiCMS, SDS-PAGE
56000
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determined by SDS-PAGE
60000
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x * 60000, recombinant His6-tagged enzyme, SDS-PAGE
120000
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wild-type full-length, Zn2+ removed by EDTA, gel filtration analysis
128000
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H400A/H408A mutant enzyme (preventing Zn2+-binding), gel filtration analysis
310000
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wild-type full-length, gel filtration analysis
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
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x * 60000, recombinant His6-tagged enzyme, SDS-PAGE
dimer
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2 * 120000, a tetramer of 2 head to head dimers of the smaller subunit LiCMSC are formed in the presence of Zn2+; H400A/H408A mutant in solution, gel filtration
homodimer
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catalytic domain consists of a TIM barrel flanked by an extended C-terminal region. It forms a homodimer in the crystal structure, and the active site is located at the centre of the TIM barrel near the C-terminal ends of the beta-strands and is composed of conserved residues of the beta-strands of one subunit and the C-terminal region of the other
tetramer
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purified wild-type in solution, gel filtration. Is presumably a tetramer due to the presence of Zn2+ co-purified with the enzyme from the expression system
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
C-terminal regulatory domain of CMS (CMSC) in complex with isoleucine, by hanging-drop vapour diffusion method. Crystals of CMSC belong to space group C222 (type I) with unit cell parameters a = 62.6 A, b = 98.4 A and c = 40.1 A, refined to 2.5 A resolution. Type II crystals of CMSC grown at room temperature belong to space group C2 with unit cell parameters a = 61.3 A, b = 97.9 A, c = 40.0 A and beta = 91.4, refined to 2.0 A resolution. Type III crystals of CMSC grown at 4°C belong to space group C222 with unit cell parameters a = 108.2 A, b = 118.6 A and c = 63.6 A, refined to 2.7 A resolution. CMSC consists of six beta-strands forming two anti-parallel beta-sheets and two alpha-helices and assumes a betaalphabeta three-layer sandwich structure. The inhibitor isoleucine is bound in a pocket at the dimer interface and has both hydrophobic and hydrogen-bonding interactions with several conserved residues of both subunits; hanging-drop vapor diffusion, in 20 mM Tris-HCl, pH 8.4 with 50 mM NaCl
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full-length LiCMS protein is used for the crystallization experiments, which are performed at room temperature (20°C) using the hanging-drop vapour-diffusion method. Crystal structures of the catalytic domain of LiCMS and its complexes with substrates; the crystal structures of LiCMSN, the N-terminal catalytic domain, in complex with malonate at 2.0 A resolution, in complex with pyruvate at 2.6 A resolution, and in complex with pyruvate and acetyl-CoA at 2.5 A are reported; the crystal structures of the catalytic domains of LiCMS and its complexes with substrates are solved
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0 - 40
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80% of maximal activity within this range
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
; full-length and mutant CMS
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; recombinant His6-tagged enzyme 14.3fold from Escherichia coli by nickel affinity chromatography to homogeneity
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affinity chromatography using a Ni2+-NTA (Ni2+-nitrilotriacetate) Superflow column; by affinity chromatography using a Ni2+-NTA Superflow column, the N-terminal His6-tag is removed by thrombin digestion, subsequently an anion-exchange Q-column is applied; using a Ni2+-NTA Superflow column and an anion-exchange Q-column, the tag is removed by cleavage with thrombin
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by using Ni-nitrilotriacetic spin columns; with Ni-nitrilotriacetic acid spin columns
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cells are centrifuged, pellet sonicated, resuspended in 0.1 M N-tris(hydroxymethyl)methyl-2-aminoethanesulfonic acid buffer, pH 7.5
recombinant CimA 26.5fold from Escherichia coli strain BL21(DE3) by ammonium sulfate fractionation and heat treatment at 60°C for 10 min, followed by gel filtration
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
; full-length and mutant CMS
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expressed in Escherichia coli; expression in Escherichia coli BL21 Star DE3 cells
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expressed in Escherichia coli; into the pET-28b vector for expression in Escherichia coli BL21DE3 cells; into the vector pET-28b for expression of the protein in Escherichia coli BL21DE3 cells
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expression in Escherichia coli; gene cimA, DNA and amino acid sequence determination and analysis, expression as His6-tagged enzyme in Escherichia coli
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gene MJ1392 or cimA, DNA and amino acid sequence determination and analysis, functional overexpression in Escherichia coli strain BL21(DE3)
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D17A
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construct for kinetic and mutagenesis studies of LiCMS; LiCMS mutant, caused a 34fold increase in the Km for pyruvate, and a 315fold decrease in the kcat; mutation of the active site
D17N
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construct for kinetic and mutagenesis studies of LiCMS; LiCMS mutant, causes a 4.4fold increase in the Km for pyruvate, and a 480fold decrease in the kcat; mutation of the active site
D304A
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LiCMS mutant, substantially weakens the binding of both acetyl-CoA and pyruvate and also decrease the kcat value; mutation in the C-regional region of LiCMSN
D404A
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construct for kinetic and mutagenesis studies of LiCMS
D431A
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changes hydrophobic residues at inhibitor binding site, minor effect on Km for acetyl-CoA but moderate decrease of kcat in the absence of inhibitor isoleucine, severely decreased inhibition by isoleucine (increase of IC50 and Ki values); has markedly increased IC50 and Ki values for isoleucine
E146D
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construct for kinetic and mutagenesis studies of LiCMS; LiCMS mutant, minor effects on the binding of acetyl-CoA, but can cause a decrease in the kcat by more than 400fold; mutation of the active site
E146Q
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construct for kinetic and mutagenesis studies of LiCMS; LiCMS mutant, minor effects on the binding of acetyl-CoA, but can cause a decrease in the kcat by more than 400fold; mutation of the active site
F83A
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construct for kinetic and mutagenesis studies of LiCMS; LiCMS mutant, results in a 5fold increase in the Km for acetyl-CoA and a 120fold decrease in the kcat; mutation of the active site
H302A/H302N
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construct for kinetic and mutagenesis studies of LiCMS; LiCMS mutant, disrupts the enzymatic activity of LiCMS; mutation in the C-regional region of LiCMSN
H400A/H408A
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prevents Zn2+-binding and enables dimer instead of tetramer formation, no change in enzymatic activity or the inhibition by isoleucine
H400A/H408A mutant
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exists purely as a dimer in solution. Is inhibited by isoleucine with comparable IC50 and Ki values as the wild-type enzyme, the double mutations have very little effects on the binding (Km) of acetyl-CoA and the kcat. Binding of isoleucine with the mutant does not affect the dimeric state of the enzyme
I458A
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changes hydrophobic residues at inhibitor binding site, minor effect on Km for acetyl-CoA but moderate decrease of kcat in the absence of inhibitor isoleucine, no inhibition by isoleucine, no binding of isoleucine; inhibition by isoleucine is severely decreased. Lower Kcat/Km as the wild-type
L104V
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construct for kinetic and mutagenesis studies of LiCMS; LiCMS mutant; mutation of the substrate binding site
L311A
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construct for kinetic and mutagenesis studies of LiCMS; LiCMS mutant, substantially weakens the binding of both acetyl-CoA and pyruvate and also decrease the kcat value; mutation in the C-regional region of LiCMSN
L451V
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changes hydrophobic residues at inhibitor binding site, minor effect on Km for acetyl-CoA but moderate decrease of kcat in the absence of inhibitor isoleucine, severely decreased inhibition by isoleucine (increase of IC50 and Ki values); inhibition by isoleucine is severely decreased
L81A
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construct for kinetic and mutagenesis studies of LiCMS; LiCMS mutant; mutation of the substrate binding site
L81V
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construct for kinetic and mutagenesis studies of LiCMS; LiCMS mutant; mutation of the substrate binding site
LiCMSN
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truncation mutant, N-terminal catalytic domain of LiCMS. Although LiCMSN can bind both pyruvate and acetyl-CoA, it is enzymatically inactive. Binding affinities of LiCMSN for acetyl-CoA and pyruvate are decreased by approx. 5fold and 2.5fold respectively compared with those of the full-length enzyme
LiCMSN1-330
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N-terminal catalytic domain used for crystallization experiments
N310A
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construct for kinetic and mutagenesis studies of LiCMS; LiCMS mutant, has a much smaller effect on the binding of pyruvate and acetyl-CoA and on the enzymatic activity; mutation in the C-regional region of LiCMSN
P493A
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changes hydrophobic residues at inhibitor binding site, minor effect on Km for acetyl-CoA but moderate decrease of kcat in the absence of inhibitor isoleucine, severely decreased inhibition by isoleucine (increase of IC50 and Ki values); inhibition by isoleucine is greatly decreased
Q495A
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changes hydrophobic residues at inhibitor binding site, minor effect on Km for acetyl-CoA but moderate decrease of kcat in the absence of inhibitor isoleucine, severely decreased inhibition by isoleucine (increase of IC50 and Ki values); exhibits significantly increased IC50 and Ki values for isoleucine
R16K/R16Q
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construct for kinetic and mutagenesis studies of LiCMS; LiCMS mutant, abolishes the enzymatic activity of LiCMS; mutation of the active site
T179A
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construct for kinetic and mutagenesis studies of LiCMS; LiCMS mutant, resultes in a 16.4fold increase in the Km for pyruvate and a 186fold decrease in the kcat, confirming its functional role in the binding of pyruvate and the catalytic reaction; mutation of the active site
T464A
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changes hydrophobic residues at inhibitor binding site, minor effect on Km for acetyl-CoA but moderate decrease of kcat in the absence of inhibitor isoleucine, minor effect on IC50 and Ki values for isoleucine; minor effect on the IC50 and Ki values for isoleucine
V468A
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changes hydrophobic residues at inhibitor binding site, minor effect on Km for acetyl-CoA but moderate decrease of kcat in the absence of inhibitor isoleucine, slightly increased inhibition by isoleucine, and inhibition by leucine; inhibition by isoleucine is slightly decreased
Y144A
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LiCMS mutant
Y144L
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construct for kinetic and mutagenesis studies of LiCMS; LiCMS mutant; mutation of the substrate binding site
Y144V
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construct for kinetic and mutagenesis studies of LiCMS; LiCMS mutant; mutation of the substrate binding site
Y312A
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construct for kinetic and mutagenesis studies of LiCMS; LiCMS mutant, abolishes the enzymatic activity of LiCMS; mutation in the C-regional region of LiCMSN
Y430L
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changes hydrophobic residues at inhibitor binding site, minor effect on Km for acetyl-CoA but moderate decrease of kcat in the absence of inhibitor isoleucine, severely decreased inhibition by isoleucine (increase of IC50 and Ki values); inhibition by isoleucine is severely decreased
Y454A
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changes hydrophobic residues at inhibitor binding site, minor effect on Km for acetyl-CoA but moderate decrease of kcat in the absence of inhibitor isoleucine, severely decreased inhibition by isoleucine (increase of IC50 and Ki values), slight inhibition by leucine; inhibition by isoleucine is severely decreased. Lower Kcat/Km as the wild-type
I47V/D86G/H126Q/T204A
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CimA3.5. 1-Propanol and 1-butanol production with CimA wild-type is 302 mg/l for 1-propanol and 18 mg/l for 1-butanol, production increased with CimA3.5 mutant 7.7fold for 1-propanol and 7.8fold for 1-butanol; CimA3.5, mutant generated by directed evolution
I47V/E111K/E121V/H126Q/T204A/M250V
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CimA3.8. 1-Propanol and 1-butanol production with CimA wild-type is 302 mg/l for 1-propanol and 18 mg/l for 1-butanol, production increased with CimA3.8 mutant 8.2fold for 1-propanol and 21.7fold for 1-butanol; CimA3.8, mutant generated by directed evolution
I47V/E114V/H126Q/T204A/L238S
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CimA3.7, mutant generated by directed evolution; CimA3.7, shows higher activity at all temperatures tested relative to wild-type CimA, although the difference of the specific activity is larger at lower temperature, possibly because the mutant is screened at 30°C. 1-Propanol and 1-butanol production with CimA wild-type is 302 mg/l for 1-propanol and 18 mg/l for 1-butanol, production increased with CimA3.7 mutant 9.2fold for 1-propanol and 21.9fold for 1-butanol
I47V/H126Q/D141E/T204A/I286V/L327H
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CimA3.4. 1-Propanol and 1-butanol production with CimA wild-type is 302 mg/l for 1-propanol and 18 mg/l for 1-butanol, production increased with CimA3.4 mutant 8.1fold for 1-propanol and 6.2fold for 1-butanol; CimA3.4, mutant generated by directed evolution
I47V/H126Q/E183K/T204A/L253S
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CimA3.2. 1-Propanol and 1-butanol production with CimA wild-type is 302 mg/l for 1-propanol and 18 mg/l for 1-butanol, production increased with CimA3.2 mutant 8.5fold for 1-propanol and 14.1fold for 1-butanol; CimA3.2, mutant generated by directed evolution
I47V/H126Q/T204A
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CimA2DELTA. 1-Propanol and 1-butanol production with CimA wild-type is 302 mg/l for 1-propanol and 18 mg/l for 1-butanol, production increased with CimA2DELTA mutant 8.0fold for 1-propanol and 5.9fold for 1-butanol; CimA2delta, mutant generated by directed evolution
I47V/H126Q/T204A/D328V
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CimA3.6. 1-Propanol and 1-butanol production with CimA wild-type is 302 mg/l for 1-propanol and 18 mg/l for 1-butanol, production increased with CimA3.6 mutant 7.8fold for 1-propanol and 8.0fold for 1-butanol; CimA3.6, mutant generated by directed evolution
I47V/H126Q/T204A/K265R/F349C
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CimA3.3. 1-Propanol and 1-butanol production with CimA wild-type is 302 mg/l for 1-propanol and 18 mg/l for 1-butanol, production increased with CimA3.3 mutant 7.9fold for 1-propanol and 6.9fold for 1-butanol; CimA3.3, mutant generated by directed evolution
I47V/H126Q/T204A/V373STOP
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CimA2, contains a frameshift mutation at bp 1117, creating a CimA variant missing the C-terminal domain from the 373rd residue. 1-Propanol and 1-butanol production with CimA wild-type is 302 mg/l for 1-propanol and 18 mg/l for 1-butanol, production increased with CimA2 mutant 3.9fold for 1-propanol and 4.3fold for 1-butanol; CimA2, mutant generated by directed evolution
I47V/K435N/V441A
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CimA1, leads to the highest 1-propanol production, and thus the largest 2-ketobutyrate pool and highest cimA activity. CimA1 mutant contains 3 amino acid substitutions (I47V, K435N, and V441A). 1-Propanol and 1-butanol production with CimA wild-type is 302 mg/l for 1-propanol and 18 mg/l for 1-butanol, production increased with CimA1 mutant 2.3fold for 1-propanol and 1.2fold for 1-butanol; CimA1, mutant generated by directed evolution
I47V/R53S/H126Q/T204A
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CimA3.1. 1-Propanol and 1-butanol production with CimA wild-type is 302 mg/l for 1-propanol and 18 mg/l for 1-butanol, production increased with CimA3.1 mutant 8.2fold for 1-propanol and 20.7fold for 1-butanol; CimA3.1, mutant generated by directed evolution
K32N/I47V/H126Q/T204A
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CimA3.9. 1-Propanol and 1-butanol production with CimA wild-type is 302 mg/l for 1-propanol and 18 mg/l for 1-butanol, production increased with CimA3.9 mutant 8.1fold for 1-propanol and 11.0fold for 1-butanol; CimA3.9, mutant generated by directed evolution
wild-typeDELTA
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1-Propanol and 1-butanol production with CimA wild-type is 302 mg/l for 1-propanol and 18 mg/l for 1-butanol, production increased with wild-typeDELTA mutant 0.2fold for 1-propanol, production for 1-butanol is not detected
WTDELTA
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wild-type delta, mutant generated by directed evolution
I47V/H126Q/T204A
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CimA2delta, mutant generated by directed evolution
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I47V/H126Q/T204A/V373STOP
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CimA2, contains a frameshift mutation at bp 1117, creating a CimA variant missing the C-terminal domain from the 373rd residue. 1-Propanol and 1-butanol production with CimA wild-type is 302 mg/l for 1-propanol and 18 mg/l for 1-butanol, production increased with CimA2 mutant 3.9fold for 1-propanol and 4.3fold for 1-butanol; CimA2, mutant generated by directed evolution
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I47V/K435N/V441A
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CimA1, leads to the highest 1-propanol production, and thus the largest 2-ketobutyrate pool and highest cimA activity. CimA1 mutant contains 3 amino acid substitutions (I47V, K435N, and V441A). 1-Propanol and 1-butanol production with CimA wild-type is 302 mg/l for 1-propanol and 18 mg/l for 1-butanol, production increased with CimA1 mutant 2.3fold for 1-propanol and 1.2fold for 1-butanol; CimA1, mutant generated by directed evolution
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
biofuel production
biotechnology
fermentation of C5 and C6 sugars to ethanols and other metabolites under thermophilic conditions
energy production
medicine
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catalyses the first reaction of the pathway which converts pyruvate and acetyl-CoA into citramalate, thus making it an attractive target for the development of antibacterial agents; Leptospira interrogans is the causative agent for leptospirosis, LiCMS is an atttractive target for the development of antibacterial agents
synthesis
Cyanothece sp.
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the autrotrophic micro-organism may be engineered for robust butanol and propanol production from 2-ketobutyrate, which is an intermediate in the isoleucine biosynthesis pathway
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