Literature summary for 2.3.3.21 extracted from

Ma, J.; Zhang, P.; Zhang, Z.; Zha, M.; Xu, H.; Zhao, G.; Ding, J.
Molecular basis of the substrate specificity and the catalytic mechanism of citramalate synthase from Leptospira interrogans (2008), Biochem. J., 415, 45-56.

Application

Application	Comment	Organism
medicine	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
medicine	Leptospira interrogans is the causative agent for leptospirosis, LiCMS is an atttractive target for the development of antibacterial agents	Leptospira interrogans

Cloned(Commentary)

Cloned (Comment)	Organism
expressed in Escherichia coli	Leptospira interrogans
into the pET-28b vector for expression in Escherichia coli BL21DE3 cells	Leptospira interrogans
into the vector pET-28b for expression of the protein in Escherichia coli BL21DE3 cells	Leptospira interrogans

Crystallization (Commentary)

Crystallization (Comment)	Organism
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	Leptospira interrogans
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	Leptospira interrogans
the crystal structures of the catalytic domains of LiCMS and its complexes with substrates are solved	Leptospira interrogans

Protein Variants

Protein Variants	Comment	Organism
D17A	mutation of the active site	Leptospira interrogans
D17A	construct for kinetic and mutagenesis studies of LiCMS	Leptospira interrogans
D17A	LiCMS mutant, caused a 34fold increase in the Km for pyruvate, and a 315fold decrease in the kcat	Leptospira interrogans
D17N	mutation of the active site	Leptospira interrogans
D17N	construct for kinetic and mutagenesis studies of LiCMS	Leptospira interrogans
D17N	LiCMS mutant, causes a 4.4fold increase in the Km for pyruvate, and a 480fold decrease in the kcat	Leptospira interrogans
D304A	mutation in the C-regional region of LiCMSN	Leptospira interrogans
D304A	LiCMS mutant, substantially weakens the binding of both acetyl-CoA and pyruvate and also decrease the kcat value	Leptospira interrogans
D404A	construct for kinetic and mutagenesis studies of LiCMS	Leptospira interrogans
E146D	mutation of the active site	Leptospira interrogans
E146D	construct for kinetic and mutagenesis studies of LiCMS	Leptospira interrogans
E146D	LiCMS mutant, minor effects on the binding of acetyl-CoA, but can cause a decrease in the kcat by more than 400fold	Leptospira interrogans
E146Q	mutation of the active site	Leptospira interrogans
E146Q	construct for kinetic and mutagenesis studies of LiCMS	Leptospira interrogans
E146Q	LiCMS mutant, minor effects on the binding of acetyl-CoA, but can cause a decrease in the kcat by more than 400fold	Leptospira interrogans
F83A	mutation of the active site	Leptospira interrogans
F83A	construct for kinetic and mutagenesis studies of LiCMS	Leptospira interrogans
F83A	LiCMS mutant, results in a 5fold increase in the Km for acetyl-CoA and a 120fold decrease in the kcat	Leptospira interrogans
H302A/H302N	mutation in the C-regional region of LiCMSN	Leptospira interrogans
H302A/H302N	construct for kinetic and mutagenesis studies of LiCMS	Leptospira interrogans
H302A/H302N	LiCMS mutant, disrupts the enzymatic activity of LiCMS	Leptospira interrogans
L104V	mutation of the substrate binding site	Leptospira interrogans
L104V	construct for kinetic and mutagenesis studies of LiCMS	Leptospira interrogans
L104V	LiCMS mutant	Leptospira interrogans
L311A	mutation in the C-regional region of LiCMSN	Leptospira interrogans
L311A	construct for kinetic and mutagenesis studies of LiCMS	Leptospira interrogans
L311A	LiCMS mutant, substantially weakens the binding of both acetyl-CoA and pyruvate and also decrease the kcat value	Leptospira interrogans
L81A	mutation of the substrate binding site	Leptospira interrogans
L81A	construct for kinetic and mutagenesis studies of LiCMS	Leptospira interrogans
L81A	LiCMS mutant	Leptospira interrogans
L81V	mutation of the substrate binding site	Leptospira interrogans
L81V	construct for kinetic and mutagenesis studies of LiCMS	Leptospira interrogans
L81V	LiCMS mutant	Leptospira interrogans
LiCMSN	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	Leptospira interrogans
LiCMSN1-330	N-terminal catalytic domain used for crystallization experiments	Leptospira interrogans
N310A	mutation in the C-regional region of LiCMSN	Leptospira interrogans
N310A	construct for kinetic and mutagenesis studies of LiCMS	Leptospira interrogans
N310A	LiCMS mutant, has a much smaller effect on the binding of pyruvate and acetyl-CoA and on the enzymatic activity	Leptospira interrogans
R16K/R16Q	mutation of the active site	Leptospira interrogans
R16K/R16Q	construct for kinetic and mutagenesis studies of LiCMS	Leptospira interrogans
R16K/R16Q	LiCMS mutant, abolishes the enzymatic activity of LiCMS	Leptospira interrogans
T179A	mutation of the active site	Leptospira interrogans
T179A	construct for kinetic and mutagenesis studies of LiCMS	Leptospira interrogans
T179A	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	Leptospira interrogans
Y144A	LiCMS mutant	Leptospira interrogans
Y144L	mutation of the substrate binding site	Leptospira interrogans
Y144L	construct for kinetic and mutagenesis studies of LiCMS	Leptospira interrogans
Y144L	LiCMS mutant	Leptospira interrogans
Y144V	mutation of the substrate binding site	Leptospira interrogans
Y144V	construct for kinetic and mutagenesis studies of LiCMS	Leptospira interrogans
Y144V	LiCMS mutant	Leptospira interrogans
Y312A	mutation in the C-regional region of LiCMSN	Leptospira interrogans
Y312A	construct for kinetic and mutagenesis studies of LiCMS	Leptospira interrogans
Y312A	LiCMS mutant, abolishes the enzymatic activity of LiCMS	Leptospira interrogans

KM Value [mM]

KM Value [mM]	KM Value Maximum [mM]	Substrate	Comment	Organism
0.06	-	pyruvate	wild-type	Leptospira interrogans
0.06	-	pyruvate	wild type LiCMS	Leptospira interrogans
0.06	-	pyruvate	wild type, kinetic data for the C-terminal region of LiCMS	Leptospira interrogans
0.06	-	pyruvate	wild type, kinetic data for the catalytic reaction of the active site of LiCMS	Leptospira interrogans
0.06	-	pyruvate	wild type, kinetic data for the substrate-binding site of LiCMS	Leptospira interrogans
0.098	-	2-oxoisovalerate	L81A mutant	Leptospira interrogans
0.105	-	pyruvate	L104V mutant	Leptospira interrogans
0.105	-	pyruvate	L104 mutant	Leptospira interrogans
0.105	-	pyruvate	mutant L104V, kinetic data for the substrate-binding site of LiCMS	Leptospira interrogans
0.15	-	pyruvate	LiCMSN, N-terminal domain of LiCMS	Leptospira interrogans
0.15	-	pyruvate	LiCMSN mutant	Leptospira interrogans
0.15	-	pyruvate	LiCMSN, kinetic data for the catalytic reaction of the active site of LiCMS	Leptospira interrogans
0.151	-	2-oxoisovalerate	Y144L mutant	Leptospira interrogans
0.153	-	pyruvate	D304A mutant	Leptospira interrogans
0.153	-	pyruvate	mutant D304A, kinetic data for the C-terminal region of LiCMS	Leptospira interrogans
0.17	-	pyruvate	N310A mutant	Leptospira interrogans
0.17	-	pyruvate	mutant N310A, kinetic data for the C-terminal region of LiCMS	Leptospira interrogans
0.198	-	pyruvate	L81V mutant	Leptospira interrogans
0.198	-	pyruvate	mutant L81V, kinetic data for the substrate-binding site of LiCMS	Leptospira interrogans
0.253	-	2-oxoisovalerate	L104V mutant	Leptospira interrogans
0.263	-	pyruvate	D17N mutant	Leptospira interrogans
0.263	-	pyruvate	mutant D17N, kinetic data for the catalytic reaction of the active site of LiCMS	Leptospira interrogans
0.282	-	pyruvate	L81A mutant	Leptospira interrogans
0.282	-	pyruvate	mutant L81A, kinetic data for the substrate-binding site of LiCMS	Leptospira interrogans
0.465	-	2-oxobutyrate	L81A mutant	Leptospira interrogans
0.47	1	2-oxobutyrate	L104V mutant	Leptospira interrogans
0.695	-	2-oxobutyrate	wild-type	Leptospira interrogans
0.695	-	2-oxobutyrate	wild type LiCMS	Leptospira interrogans
0.979	-	pyruvate	T179A mutant	Leptospira interrogans
0.979	-	pyruvate	mutant T179A, kinetic data for the catalytic reaction of the active site of LiCMS	Leptospira interrogans
1.023	-	glyoxylate	Y144V mutant	Leptospira interrogans
1.118	-	acetyl-CoA	wild-type	Leptospira interrogans
1.118	-	acetyl-CoA	wild type LiCMS	Leptospira interrogans
1.118	-	acetyl-CoA	wild type, kinetic data for the C-terminal region of LiCMS	Leptospira interrogans
1.118	-	acetyl-CoA	wild type, kinetic data for the catalytic reaction of the active site of LiCMS	Leptospira interrogans
1.118	-	acetyl-CoA	wild type, kinetic data for the substrate-binding site of LiCMS	Leptospira interrogans
1.137	-	acetyl-CoA	L81A mutant	Leptospira interrogans
1.137	-	acetyl-CoA	mutant L81A, kinetic data for the substrate-binding site of LiCMS	Leptospira interrogans
1.214	-	acetyl-CoA	L81V mutant	Leptospira interrogans
1.214	-	acetyl-CoA	mutant L81V, kinetic data for the substrate-binding site of LiCMS	Leptospira interrogans
1.272	-	pyruvate	L311A mutant	Leptospira interrogans
1.272	-	pyruvate	mutant L311A, kinetic data for the C-terminal region of LiCMS	Leptospira interrogans
1.47	-	glyoxylate	wild-type	Leptospira interrogans
1.47	-	glyoxylate	wild type LiCMS	Leptospira interrogans
1.511	-	acetyl-CoA	E146D mutant	Leptospira interrogans
1.511	-	acetyl-CoA	mutant E146D, kinetic data for the catalytic reaction of the active site of LiCMS	Leptospira interrogans
1.691	-	acetyl-CoA	Y144V mutant	Leptospira interrogans
1.691	-	acetyl-CoA	mutant Y144V, kinetic data for the substrate-binding site of LiCMS	Leptospira interrogans
1.904	-	acetyl-CoA	Y144L mutant	Leptospira interrogans
1.904	-	acetyl-CoA	mutant Y144L, kinetic data for the substrate-binding site of LiCMS	Leptospira interrogans
2.036	-	pyruvate	D17A mutant	Leptospira interrogans
2.036	-	pyruvate	mutant D17A, kinetic data for the catalytic reaction of the active site of LiCMS	Leptospira interrogans
2.391	-	acetyl-CoA	E146Q mutant	Leptospira interrogans
2.391	-	acetyl-CoA	mutant E146Q, kinetic data for the catalytic reaction of the active site of LiCMS	Leptospira interrogans
2.409	-	acetyl-CoA	N310A mutant	Leptospira interrogans
2.409	-	acetyl-CoA	mutant N310A, kinetic data for the C-terminal region of LiCMS	Leptospira interrogans
2.898	-	glyoxylate	L104V mutant	Leptospira interrogans
2.924	-	2-oxobutyrate	L81V mutant	Leptospira interrogans
3.028	-	acetyl-CoA	L104V mutant	Leptospira interrogans
3.028	-	acetyl-CoA	mutant L104V, kinetic data for the substrate-binding site of LiCMS	Leptospira interrogans
3.498	-	glyoxylate	Y144L mutant	Leptospira interrogans
5.186	-	acetyl-CoA	R16K/R16Q mutant	Leptospira interrogans
5.186	-	acetyl-CoA	F83A mutant	Leptospira interrogans
5.186	-	acetyl-CoA	mutant F83A, kinetic data for the catalytic reaction of the active site of LiCMS	Leptospira interrogans
5.273	-	acetyl-CoA	LiCMSN, N-terminal domain of LiCMS	Leptospira interrogans
5.273	-	acetyl-CoA	LiCMSN mutant	Leptospira interrogans
5.273	-	acetyl-CoA	LiCMSN, kinetic data for the catalytic reaction of the active site of LiCMS	Leptospira interrogans
5.851	-	acetyl-CoA	D304A mutant	Leptospira interrogans
5.851	-	acetyl-CoA	mutant D304A, kinetic data for the C-terminal region of LiCMS	Leptospira interrogans
6.519	-	2-oxobutyrate	Y144V mutant	Leptospira interrogans
6.859	-	pyruvate	Y144V mutant	Leptospira interrogans
6.859	-	pyruvate	mutant Y144V, kinetic data for the substrate-binding site of LiCMS	Leptospira interrogans
7.225	-	glyoxylate	L81V mutant	Leptospira interrogans
8.921	-	acetyl-CoA	L311A mutant	Leptospira interrogans
8.921	-	acetyl-CoA	mutant L311A, kinetic data for the C-terminal region of LiCMS	Leptospira interrogans
10.6	-	glyoxylate	L81A mutant	Leptospira interrogans
12.61	-	2-oxobutyrate	Y144L mutant	Leptospira interrogans
15.53	-	pyruvate	Y144L mutant	Leptospira interrogans
15.53	-	pyruvate	mutant Y144L, kinetic data for the substrate-binding site of LiCMS	Leptospira interrogans
52.85	-	2-oxoisovalerate	Y144V mutant	Leptospira interrogans

Metals/Ions

Metals/Ions	Comment	Organism
Ca2+	-	Leptospira interrogans
Ca2+	enzymatic activity of LiCMS in the absence and presence of different metal ions. Ca2+ is an activator	Leptospira interrogans
Co2+	-	Leptospira interrogans
Co2+	enzymatic activity of LiCMS in the absence and presence of different metal ions. Co2+ is an activator	Leptospira interrogans
Cu2+	enzymatic activity of LiCMS in the absence and presence of different metal ions. Cu2+ is an inhibitor	Leptospira interrogans
K+	-	Leptospira interrogans
K+	enzymatic activity of LiCMS in the absence and presence of different metal ions. Co-activation by K+ in the presence of Mn2+	Leptospira interrogans
Li+	-	Leptospira interrogans
Mg2+	-	Leptospira interrogans
Mg2+	enzymatic activity of LiCMS in the absence and presence of different metal ions. Mg2+ is an activator	Leptospira interrogans
Mn2+	-	Leptospira interrogans
Mn2+	enzymatic activity of LiCMS in the absence and presence of different metal ions. Enzyme shows the highest activity in the presence of Mn2+. Coactivation by K+	Leptospira interrogans
Na+	-	Leptospira interrogans
NH4+	-	Leptospira interrogans
NH4+	can act as a co-activator in the presence of Mn2+	Leptospira interrogans
Ni2+	-	Leptospira interrogans
Ni2+	enzymatic activity of LiCMS in the absence and presence of different metal ions. Ni2+ is an activator	Leptospira interrogans
Zn2+	enzymatic activity of LiCMS in the absence and presence of different metal ions. Zn2+ is an inhibitor	Leptospira interrogans

Molecular Weight [Da]

Molecular Weight [Da]	Molecular Weight Maximum [Da]	Comment	Organism
14000	-	corresponds to the C-terminal regulatory domain of LiCMS, SDS-PAGE	Leptospira interrogans
33000	-	corresponds to the N-terminal catalytic domain of LiCMS, SDS-PAGE	Leptospira interrogans
56000	-	determined by SDS-PAGE	Leptospira interrogans

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
(2S)-2-hydroxy-2-methylbutanedioate	Leptospira interrogans	-	acetate + pyruvate	-	r
acetyl-CoA + pyruvate + H2O	Leptospira interrogans	-	CoA + (2R)-2-hydroxy-2-methylbutanedioate	-	?

Organism

Organism	UniProt	Comment	Textmining
Leptospira interrogans	-	-	-

Purification (Commentary)

Purification (Comment)	Organism
affinity chromatography using a Ni2+-NTA (Ni2+-nitrilotriacetate) Superflow column	Leptospira interrogans
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	Leptospira interrogans
using a Ni2+-NTA Superflow column and an anion-exchange Q-column, the tag is removed by cleavage with thrombin	Leptospira interrogans

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg]	Specific Activity Maximum [µmol/min/mg]	Comment	Organism
additional information	-	specific activity for Zn2+ -0.04 micromol/min/mg and -0.13 micromol/min/mg for Cu2+	Leptospira interrogans
0.2	-	in the absence of metal ions	Leptospira interrogans
0.2	-	without metals	Leptospira interrogans
0.4	-	in the presence of K+	Leptospira interrogans
0.4	-	with K+	Leptospira interrogans
1.1	-	in the presence of Ni2+	Leptospira interrogans
1.1	-	with Ni2+	Leptospira interrogans
1.2	-	with Mg2+	Leptospira interrogans
1.2	-	in the presence of Mg2+	Leptospira interrogans
2.2	-	in the presence of Ca2+	Leptospira interrogans
2.2	-	with Ca2+	Leptospira interrogans
2.5	-	in the presence of Co2+	Leptospira interrogans
2.5	-	with Co2+	Leptospira interrogans
6.1	-	in the presence of Mn2+ and Li+	Leptospira interrogans
6.1	-	with Li+	Leptospira interrogans
6.2	-	with Mn2+	Leptospira interrogans
6.2	-	in the presence of Mn2+	Leptospira interrogans
6.5	-	in the presence of Mn2+ and Na+	Leptospira interrogans
6.5	-	with Na+	Leptospira interrogans
7.1	-	with Mn2+	Leptospira interrogans
7.1	-	in the presence of Mn2+	Leptospira interrogans
9	-	in the presence of Mn2+ and NH4+	Leptospira interrogans
9	-	with NH4+	Leptospira interrogans
9.4	-	in the presence of Mn2+ and K+	Leptospira interrogans
9.4	-	with K+	Leptospira interrogans

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.
(2S)-2-hydroxy-2-methylbutanedioate	-	Leptospira interrogans	acetate + pyruvate	-	r
acetyl-CoA + 2-oxobutyrate + H2O	-	Leptospira interrogans	?	-	?
acetyl-CoA + 2-oxoisovalerate + H2O	-	Leptospira interrogans	?	-	?
acetyl-CoA + glyoxylate + H2O	-	Leptospira interrogans	?	-	?
acetyl-CoA + pyruvate + H2O	-	Leptospira interrogans	CoA + (2R)-2-hydroxy-2-methylbutanedioate	-	?
acetyl-CoA + pyruvate + H2O	-	Leptospira interrogans	CoA + (R)-citramalate	-	?
acetyl-CoA + pyruvate + H2O	-	Leptospira interrogans	(2S)-2-hydroxy-2-methylbutanedioate + CoA	-	r
additional information	LiCMS shows high substrate specificity for pyruvate, but has very weak or no detectable activities for other alpha-oxo acids, such as glyoxylate, 2-oxobutyrate, and 2-oxoisovalerate	Leptospira interrogans	?	-	?

Subunits

Subunits	Comment	Organism
homodimer	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	Leptospira interrogans

Synonyms

Synonyms	Comment	Organism
citramalate lyase	-	Leptospira interrogans
citramalate synthase	-	Leptospira interrogans
LiCMS	-	Leptospira interrogans

Temperature Optimum [°C]

Temperature Optimum [°C]	Temperature Optimum Maximum [°C]	Comment	Organism
37	-	activity assay	Leptospira interrogans
37	-	enzymatic activity assay	Leptospira interrogans

Turnover Number [1/s]

Turnover Number Minimum [1/s]	Turnover Number Maximum [1/s]	Substrate	Comment	Organism
0.005	-	glyoxylate	Y144L mutant	Leptospira interrogans
0.005	-	2-oxobutyrate	Y144L mutant	Leptospira interrogans
0.014	-	2-oxobutyrate	L81V mutant	Leptospira interrogans
0.017	-	acetyl-CoA	Y144L mutant	Leptospira interrogans
0.017	-	acetyl-CoA	mutant Y144L, kinetic data for the substrate-binding site of LiCMS	Leptospira interrogans
0.018	-	2-oxoisovalerate	L81A mutant	Leptospira interrogans
0.023	-	2-oxoisovalerate	Y144L mutant	Leptospira interrogans
0.03	-	2-oxobutyrate	L104V mutant	Leptospira interrogans
0.03	-	2-oxoisovalerate	L104V mutant	Leptospira interrogans
0.03	-	glyoxylate	Y144V mutant	Leptospira interrogans
0.05	-	2-oxobutyrate	L81A mutant	Leptospira interrogans
0.062	-	2-oxoisovalerate	Y144V mutant	Leptospira interrogans
0.09	-	2-oxobutyrate	wild-type	Leptospira interrogans
0.09	-	2-oxobutyrate	wild type LiCMS	Leptospira interrogans
0.12	-	pyruvate	Y144L mutant	Leptospira interrogans
0.12	-	pyruvate	mutant Y144L, kinetic data for the substrate-binding site of LiCMS	Leptospira interrogans
0.19	-	glyoxylate	L81A mutant	Leptospira interrogans
0.21	-	glyoxylate	L81V mutant	Leptospira interrogans
0.32	-	pyruvate	D304A mutant	Leptospira interrogans
0.32	-	pyruvate	mutant D304A, kinetic data for the C-terminal region of LiCMS	Leptospira interrogans
0.4	-	pyruvate	LiCMSN, N-terminal domain of LiCMS	Leptospira interrogans
0.4	-	pyruvate	LiCMSN mutant	Leptospira interrogans
0.4	-	pyruvate	LiCMSN, kinetic data for the catalytic reaction of the active site of LiCMS	Leptospira interrogans
0.51	-	glyoxylate	wild-type	Leptospira interrogans
0.51	-	glyoxylate	wild type LiCMS	Leptospira interrogans
0.58	-	pyruvate	L81A mutant	Leptospira interrogans
0.58	-	pyruvate	mutant L81A, kinetic data for the substrate-binding site of LiCMS	Leptospira interrogans
0.6	-	glyoxylate	L104V mutant	Leptospira interrogans
0.6	-	acetyl-CoA	Y144V mutant	Leptospira interrogans
0.6	-	acetyl-CoA	mutant Y144V, kinetic data for the substrate-binding site of LiCMS	Leptospira interrogans
0.62	-	acetyl-CoA	D304A mutant	Leptospira interrogans
0.62	-	2-oxobutyrate	Y144V mutant	Leptospira interrogans
0.62	-	acetyl-CoA	mutant D304A, kinetic data for the C-terminal region of LiCMS	Leptospira interrogans
0.7	-	acetyl-CoA	L81A mutant	Leptospira interrogans
0.7	-	acetyl-CoA	mutant L81A, kinetic data for the substrate-binding site of LiCMS	Leptospira interrogans
0.9	-	pyruvate	L81V mutant	Leptospira interrogans
0.9	-	pyruvate	mutant L81V, kinetic data for the substrate-binding site of LiCMS	Leptospira interrogans
1.1	-	acetyl-CoA	L81V mutant	Leptospira interrogans
1.1	-	acetyl-CoA	LiCMSN, N-terminal domain of LiCMS	Leptospira interrogans
1.1	-	acetyl-CoA	LiCMSN mutant	Leptospira interrogans
1.1	-	acetyl-CoA	LiCMSN, kinetic data for the catalytic reaction of the active site of LiCMS	Leptospira interrogans
1.1	-	acetyl-CoA	mutant L81V, kinetic data for the substrate-binding site of LiCMS	Leptospira interrogans
1.7	-	acetyl-CoA	L311A mutant	Leptospira interrogans
1.7	-	pyruvate	L311A mutant	Leptospira interrogans
1.7	-	pyruvate	Y144V mutant	Leptospira interrogans
1.7	-	acetyl-CoA	mutant L311A, kinetic data for the C-terminal region of LiCMS	Leptospira interrogans
1.7	-	pyruvate	mutant L311A, kinetic data for the C-terminal region of LiCMS	Leptospira interrogans
1.7	-	pyruvate	mutant Y144V, kinetic data for the substrate-binding site of LiCMS	Leptospira interrogans
1.9	-	pyruvate	D17N mutant	Leptospira interrogans
1.9	-	pyruvate	mutant D17N, kinetic data for the catalytic reaction of the active site of LiCMS	Leptospira interrogans
2.1	-	acetyl-CoA	E146D mutant	Leptospira interrogans
2.1	-	acetyl-CoA	mutant E146D, kinetic data for the catalytic reaction of the active site of LiCMS	Leptospira interrogans
2.4	-	acetyl-CoA	E146Q mutant	Leptospira interrogans
2.4	-	acetyl-CoA	mutant E146Q, kinetic data for the catalytic reaction of the active site of LiCMS	Leptospira interrogans
2.7	-	pyruvate	L104V mutant	Leptospira interrogans
2.7	-	pyruvate	mutant L104V, kinetic data for the substrate-binding site of LiCMS	Leptospira interrogans
2.9	-	pyruvate	D17A mutant	Leptospira interrogans
2.9	-	pyruvate	mutant D17A, kinetic data for the catalytic reaction of the active site of LiCMS	Leptospira interrogans
3.8	-	pyruvate	N310A mutant	Leptospira interrogans
3.8	-	pyruvate	mutant N310A, kinetic data for the C-terminal region of LiCMS	Leptospira interrogans
3.9	-	acetyl-CoA	L104V mutant	Leptospira interrogans
3.9	-	acetyl-CoA	mutant L104V, kinetic data for the substrate-binding site of LiCMS	Leptospira interrogans
4.9	-	pyruvate	T179A mutant	Leptospira interrogans
4.9	-	pyruvate	mutant T179A, kinetic data for the catalytic reaction of the active site of LiCMS	Leptospira interrogans
5.9	-	acetyl-CoA	N310A mutant	Leptospira interrogans
5.9	-	acetyl-CoA	mutant N310A, kinetic data for the C-terminal region of LiCMS	Leptospira interrogans
8.5	-	acetyl-CoA	R16K/R16Q mutant	Leptospira interrogans
8.5	-	acetyl-CoA	F83A mutant	Leptospira interrogans
8.5	-	acetyl-CoA	mutant F83A, kinetic data for the catalytic reaction of the active site of LiCMS	Leptospira interrogans
9.1	-	pyruvate	wild type LiCMS	Leptospira interrogans
9.1	-	pyruvate	wild type, kinetic data for the C-terminal region of LiCMS	Leptospira interrogans
9.1	-	pyruvate	wild type, kinetic data for the substrate-binding site of LiCMS	Leptospira interrogans
9.13	-	pyruvate	wild-type	Leptospira interrogans
9.13	-	pyruvate	wild type LiCMS	Leptospira interrogans
9.13	-	pyruvate	wild type, kinetic data for the catalytic reaction of the active site of LiCMS	Leptospira interrogans
10.3	-	acetyl-CoA	wild-type	Leptospira interrogans
10.3	-	acetyl-CoA	wild type LiCMS	Leptospira interrogans
10.3	-	acetyl-CoA	wild type, kinetic data for the C-terminal region of LiCMS	Leptospira interrogans
10.3	-	acetyl-CoA	wild type, kinetic data for the catalytic reaction of the active site of LiCMS	Leptospira interrogans
10.3	-	acetyl-CoA	wild type, kinetic data for the substrate-binding site of LiCMS	Leptospira interrogans

pH Optimum

pH Optimum Minimum	pH Optimum Maximum	Comment	Organism
7.7	-	activity assay	Leptospira interrogans
7.7	-	enzymatic activity assay	Leptospira interrogans