EC Number | Application | Comment | Organism |
---|---|---|---|
2.3.3.21 | 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 |
2.3.3.21 | medicine | Leptospira interrogans is the causative agent for leptospirosis, LiCMS is an atttractive target for the development of antibacterial agents | Leptospira interrogans |
EC Number | Cloned (Comment) | Organism |
---|---|---|
2.3.3.21 | expressed in Escherichia coli | Leptospira interrogans |
2.3.3.21 | into the pET-28b vector for expression in Escherichia coli BL21DE3 cells | Leptospira interrogans |
2.3.3.21 | into the vector pET-28b for expression of the protein in Escherichia coli BL21DE3 cells | Leptospira interrogans |
EC Number | Crystallization (Comment) | Organism |
---|---|---|
2.3.3.21 | 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 |
2.3.3.21 | 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 |
2.3.3.21 | the crystal structures of the catalytic domains of LiCMS and its complexes with substrates are solved | Leptospira interrogans |
EC Number | Protein Variants | Comment | Organism |
---|---|---|---|
2.3.3.21 | D17A | mutation of the active site | Leptospira interrogans |
2.3.3.21 | D17A | construct for kinetic and mutagenesis studies of LiCMS | Leptospira interrogans |
2.3.3.21 | D17A | LiCMS mutant, caused a 34fold increase in the Km for pyruvate, and a 315fold decrease in the kcat | Leptospira interrogans |
2.3.3.21 | D17N | mutation of the active site | Leptospira interrogans |
2.3.3.21 | D17N | construct for kinetic and mutagenesis studies of LiCMS | Leptospira interrogans |
2.3.3.21 | D17N | LiCMS mutant, causes a 4.4fold increase in the Km for pyruvate, and a 480fold decrease in the kcat | Leptospira interrogans |
2.3.3.21 | D304A | mutation in the C-regional region of LiCMSN | Leptospira interrogans |
2.3.3.21 | D304A | LiCMS mutant, substantially weakens the binding of both acetyl-CoA and pyruvate and also decrease the kcat value | Leptospira interrogans |
2.3.3.21 | D404A | construct for kinetic and mutagenesis studies of LiCMS | Leptospira interrogans |
2.3.3.21 | E146D | mutation of the active site | Leptospira interrogans |
2.3.3.21 | E146D | construct for kinetic and mutagenesis studies of LiCMS | Leptospira interrogans |
2.3.3.21 | 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 |
2.3.3.21 | E146Q | mutation of the active site | Leptospira interrogans |
2.3.3.21 | E146Q | construct for kinetic and mutagenesis studies of LiCMS | Leptospira interrogans |
2.3.3.21 | 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 |
2.3.3.21 | F83A | mutation of the active site | Leptospira interrogans |
2.3.3.21 | F83A | construct for kinetic and mutagenesis studies of LiCMS | Leptospira interrogans |
2.3.3.21 | F83A | LiCMS mutant, results in a 5fold increase in the Km for acetyl-CoA and a 120fold decrease in the kcat | Leptospira interrogans |
2.3.3.21 | H302A/H302N | mutation in the C-regional region of LiCMSN | Leptospira interrogans |
2.3.3.21 | H302A/H302N | construct for kinetic and mutagenesis studies of LiCMS | Leptospira interrogans |
2.3.3.21 | H302A/H302N | LiCMS mutant, disrupts the enzymatic activity of LiCMS | Leptospira interrogans |
2.3.3.21 | L104V | mutation of the substrate binding site | Leptospira interrogans |
2.3.3.21 | L104V | construct for kinetic and mutagenesis studies of LiCMS | Leptospira interrogans |
2.3.3.21 | L104V | LiCMS mutant | Leptospira interrogans |
2.3.3.21 | L311A | mutation in the C-regional region of LiCMSN | Leptospira interrogans |
2.3.3.21 | L311A | construct for kinetic and mutagenesis studies of LiCMS | Leptospira interrogans |
2.3.3.21 | L311A | LiCMS mutant, substantially weakens the binding of both acetyl-CoA and pyruvate and also decrease the kcat value | Leptospira interrogans |
2.3.3.21 | L81A | mutation of the substrate binding site | Leptospira interrogans |
2.3.3.21 | L81A | construct for kinetic and mutagenesis studies of LiCMS | Leptospira interrogans |
2.3.3.21 | L81A | LiCMS mutant | Leptospira interrogans |
2.3.3.21 | L81V | mutation of the substrate binding site | Leptospira interrogans |
2.3.3.21 | L81V | construct for kinetic and mutagenesis studies of LiCMS | Leptospira interrogans |
2.3.3.21 | L81V | LiCMS mutant | Leptospira interrogans |
2.3.3.21 | 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 |
2.3.3.21 | LiCMSN1-330 | N-terminal catalytic domain used for crystallization experiments | Leptospira interrogans |
2.3.3.21 | N310A | mutation in the C-regional region of LiCMSN | Leptospira interrogans |
2.3.3.21 | N310A | construct for kinetic and mutagenesis studies of LiCMS | Leptospira interrogans |
2.3.3.21 | N310A | LiCMS mutant, has a much smaller effect on the binding of pyruvate and acetyl-CoA and on the enzymatic activity | Leptospira interrogans |
2.3.3.21 | R16K/R16Q | mutation of the active site | Leptospira interrogans |
2.3.3.21 | R16K/R16Q | construct for kinetic and mutagenesis studies of LiCMS | Leptospira interrogans |
2.3.3.21 | R16K/R16Q | LiCMS mutant, abolishes the enzymatic activity of LiCMS | Leptospira interrogans |
2.3.3.21 | T179A | mutation of the active site | Leptospira interrogans |
2.3.3.21 | T179A | construct for kinetic and mutagenesis studies of LiCMS | Leptospira interrogans |
2.3.3.21 | 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 |
2.3.3.21 | Y144A | LiCMS mutant | Leptospira interrogans |
2.3.3.21 | Y144L | mutation of the substrate binding site | Leptospira interrogans |
2.3.3.21 | Y144L | construct for kinetic and mutagenesis studies of LiCMS | Leptospira interrogans |
2.3.3.21 | Y144L | LiCMS mutant | Leptospira interrogans |
2.3.3.21 | Y144V | mutation of the substrate binding site | Leptospira interrogans |
2.3.3.21 | Y144V | construct for kinetic and mutagenesis studies of LiCMS | Leptospira interrogans |
2.3.3.21 | Y144V | LiCMS mutant | Leptospira interrogans |
2.3.3.21 | Y312A | mutation in the C-regional region of LiCMSN | Leptospira interrogans |
2.3.3.21 | Y312A | construct for kinetic and mutagenesis studies of LiCMS | Leptospira interrogans |
2.3.3.21 | Y312A | LiCMS mutant, abolishes the enzymatic activity of LiCMS | Leptospira interrogans |
EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
2.3.3.21 | 0.06 | - |
pyruvate | wild-type | Leptospira interrogans | |
2.3.3.21 | 0.06 | - |
pyruvate | wild type LiCMS | Leptospira interrogans | |
2.3.3.21 | 0.06 | - |
pyruvate | wild type, kinetic data for the C-terminal region of LiCMS | Leptospira interrogans | |
2.3.3.21 | 0.06 | - |
pyruvate | wild type, kinetic data for the catalytic reaction of the active site of LiCMS | Leptospira interrogans | |
2.3.3.21 | 0.06 | - |
pyruvate | wild type, kinetic data for the substrate-binding site of LiCMS | Leptospira interrogans | |
2.3.3.21 | 0.098 | - |
2-oxoisovalerate | L81A mutant | Leptospira interrogans | |
2.3.3.21 | 0.105 | - |
pyruvate | L104V mutant | Leptospira interrogans | |
2.3.3.21 | 0.105 | - |
pyruvate | L104 mutant | Leptospira interrogans | |
2.3.3.21 | 0.105 | - |
pyruvate | mutant L104V, kinetic data for the substrate-binding site of LiCMS | Leptospira interrogans | |
2.3.3.21 | 0.15 | - |
pyruvate | LiCMSN, N-terminal domain of LiCMS | Leptospira interrogans | |
2.3.3.21 | 0.15 | - |
pyruvate | LiCMSN mutant | Leptospira interrogans | |
2.3.3.21 | 0.15 | - |
pyruvate | LiCMSN, kinetic data for the catalytic reaction of the active site of LiCMS | Leptospira interrogans | |
2.3.3.21 | 0.151 | - |
2-oxoisovalerate | Y144L mutant | Leptospira interrogans | |
2.3.3.21 | 0.153 | - |
pyruvate | D304A mutant | Leptospira interrogans | |
2.3.3.21 | 0.153 | - |
pyruvate | mutant D304A, kinetic data for the C-terminal region of LiCMS | Leptospira interrogans | |
2.3.3.21 | 0.17 | - |
pyruvate | N310A mutant | Leptospira interrogans | |
2.3.3.21 | 0.17 | - |
pyruvate | mutant N310A, kinetic data for the C-terminal region of LiCMS | Leptospira interrogans | |
2.3.3.21 | 0.198 | - |
pyruvate | L81V mutant | Leptospira interrogans | |
2.3.3.21 | 0.198 | - |
pyruvate | mutant L81V, kinetic data for the substrate-binding site of LiCMS | Leptospira interrogans | |
2.3.3.21 | 0.253 | - |
2-oxoisovalerate | L104V mutant | Leptospira interrogans | |
2.3.3.21 | 0.263 | - |
pyruvate | D17N mutant | Leptospira interrogans | |
2.3.3.21 | 0.263 | - |
pyruvate | mutant D17N, kinetic data for the catalytic reaction of the active site of LiCMS | Leptospira interrogans | |
2.3.3.21 | 0.282 | - |
pyruvate | L81A mutant | Leptospira interrogans | |
2.3.3.21 | 0.282 | - |
pyruvate | mutant L81A, kinetic data for the substrate-binding site of LiCMS | Leptospira interrogans | |
2.3.3.21 | 0.465 | - |
2-oxobutyrate | L81A mutant | Leptospira interrogans | |
2.3.3.21 | 0.47 | 1 | 2-oxobutyrate | L104V mutant | Leptospira interrogans | |
2.3.3.21 | 0.695 | - |
2-oxobutyrate | wild-type | Leptospira interrogans | |
2.3.3.21 | 0.695 | - |
2-oxobutyrate | wild type LiCMS | Leptospira interrogans | |
2.3.3.21 | 0.979 | - |
pyruvate | T179A mutant | Leptospira interrogans | |
2.3.3.21 | 0.979 | - |
pyruvate | mutant T179A, kinetic data for the catalytic reaction of the active site of LiCMS | Leptospira interrogans | |
2.3.3.21 | 1.023 | - |
glyoxylate | Y144V mutant | Leptospira interrogans | |
2.3.3.21 | 1.118 | - |
acetyl-CoA | wild-type | Leptospira interrogans | |
2.3.3.21 | 1.118 | - |
acetyl-CoA | wild type LiCMS | Leptospira interrogans | |
2.3.3.21 | 1.118 | - |
acetyl-CoA | wild type, kinetic data for the C-terminal region of LiCMS | Leptospira interrogans | |
2.3.3.21 | 1.118 | - |
acetyl-CoA | wild type, kinetic data for the catalytic reaction of the active site of LiCMS | Leptospira interrogans | |
2.3.3.21 | 1.118 | - |
acetyl-CoA | wild type, kinetic data for the substrate-binding site of LiCMS | Leptospira interrogans | |
2.3.3.21 | 1.137 | - |
acetyl-CoA | L81A mutant | Leptospira interrogans | |
2.3.3.21 | 1.137 | - |
acetyl-CoA | mutant L81A, kinetic data for the substrate-binding site of LiCMS | Leptospira interrogans | |
2.3.3.21 | 1.214 | - |
acetyl-CoA | L81V mutant | Leptospira interrogans | |
2.3.3.21 | 1.214 | - |
acetyl-CoA | mutant L81V, kinetic data for the substrate-binding site of LiCMS | Leptospira interrogans | |
2.3.3.21 | 1.272 | - |
pyruvate | L311A mutant | Leptospira interrogans | |
2.3.3.21 | 1.272 | - |
pyruvate | mutant L311A, kinetic data for the C-terminal region of LiCMS | Leptospira interrogans | |
2.3.3.21 | 1.47 | - |
glyoxylate | wild-type | Leptospira interrogans | |
2.3.3.21 | 1.47 | - |
glyoxylate | wild type LiCMS | Leptospira interrogans | |
2.3.3.21 | 1.511 | - |
acetyl-CoA | E146D mutant | Leptospira interrogans | |
2.3.3.21 | 1.511 | - |
acetyl-CoA | mutant E146D, kinetic data for the catalytic reaction of the active site of LiCMS | Leptospira interrogans | |
2.3.3.21 | 1.691 | - |
acetyl-CoA | Y144V mutant | Leptospira interrogans | |
2.3.3.21 | 1.691 | - |
acetyl-CoA | mutant Y144V, kinetic data for the substrate-binding site of LiCMS | Leptospira interrogans | |
2.3.3.21 | 1.904 | - |
acetyl-CoA | Y144L mutant | Leptospira interrogans | |
2.3.3.21 | 1.904 | - |
acetyl-CoA | mutant Y144L, kinetic data for the substrate-binding site of LiCMS | Leptospira interrogans | |
2.3.3.21 | 2.036 | - |
pyruvate | D17A mutant | Leptospira interrogans | |
2.3.3.21 | 2.036 | - |
pyruvate | mutant D17A, kinetic data for the catalytic reaction of the active site of LiCMS | Leptospira interrogans | |
2.3.3.21 | 2.391 | - |
acetyl-CoA | E146Q mutant | Leptospira interrogans | |
2.3.3.21 | 2.391 | - |
acetyl-CoA | mutant E146Q, kinetic data for the catalytic reaction of the active site of LiCMS | Leptospira interrogans | |
2.3.3.21 | 2.409 | - |
acetyl-CoA | N310A mutant | Leptospira interrogans | |
2.3.3.21 | 2.409 | - |
acetyl-CoA | mutant N310A, kinetic data for the C-terminal region of LiCMS | Leptospira interrogans | |
2.3.3.21 | 2.898 | - |
glyoxylate | L104V mutant | Leptospira interrogans | |
2.3.3.21 | 2.924 | - |
2-oxobutyrate | L81V mutant | Leptospira interrogans | |
2.3.3.21 | 3.028 | - |
acetyl-CoA | L104V mutant | Leptospira interrogans | |
2.3.3.21 | 3.028 | - |
acetyl-CoA | mutant L104V, kinetic data for the substrate-binding site of LiCMS | Leptospira interrogans | |
2.3.3.21 | 3.498 | - |
glyoxylate | Y144L mutant | Leptospira interrogans | |
2.3.3.21 | 5.186 | - |
acetyl-CoA | R16K/R16Q mutant | Leptospira interrogans | |
2.3.3.21 | 5.186 | - |
acetyl-CoA | F83A mutant | Leptospira interrogans | |
2.3.3.21 | 5.186 | - |
acetyl-CoA | mutant F83A, kinetic data for the catalytic reaction of the active site of LiCMS | Leptospira interrogans | |
2.3.3.21 | 5.273 | - |
acetyl-CoA | LiCMSN, N-terminal domain of LiCMS | Leptospira interrogans | |
2.3.3.21 | 5.273 | - |
acetyl-CoA | LiCMSN mutant | Leptospira interrogans | |
2.3.3.21 | 5.273 | - |
acetyl-CoA | LiCMSN, kinetic data for the catalytic reaction of the active site of LiCMS | Leptospira interrogans | |
2.3.3.21 | 5.851 | - |
acetyl-CoA | D304A mutant | Leptospira interrogans | |
2.3.3.21 | 5.851 | - |
acetyl-CoA | mutant D304A, kinetic data for the C-terminal region of LiCMS | Leptospira interrogans | |
2.3.3.21 | 6.519 | - |
2-oxobutyrate | Y144V mutant | Leptospira interrogans | |
2.3.3.21 | 6.859 | - |
pyruvate | Y144V mutant | Leptospira interrogans | |
2.3.3.21 | 6.859 | - |
pyruvate | mutant Y144V, kinetic data for the substrate-binding site of LiCMS | Leptospira interrogans | |
2.3.3.21 | 7.225 | - |
glyoxylate | L81V mutant | Leptospira interrogans | |
2.3.3.21 | 8.921 | - |
acetyl-CoA | L311A mutant | Leptospira interrogans | |
2.3.3.21 | 8.921 | - |
acetyl-CoA | mutant L311A, kinetic data for the C-terminal region of LiCMS | Leptospira interrogans | |
2.3.3.21 | 10.6 | - |
glyoxylate | L81A mutant | Leptospira interrogans | |
2.3.3.21 | 12.61 | - |
2-oxobutyrate | Y144L mutant | Leptospira interrogans | |
2.3.3.21 | 15.53 | - |
pyruvate | Y144L mutant | Leptospira interrogans | |
2.3.3.21 | 15.53 | - |
pyruvate | mutant Y144L, kinetic data for the substrate-binding site of LiCMS | Leptospira interrogans | |
2.3.3.21 | 52.85 | - |
2-oxoisovalerate | Y144V mutant | Leptospira interrogans |
EC Number | Metals/Ions | Comment | Organism | Structure |
---|---|---|---|---|
2.3.3.21 | Ca2+ | - |
Leptospira interrogans | |
2.3.3.21 | Ca2+ | enzymatic activity of LiCMS in the absence and presence of different metal ions. Ca2+ is an activator | Leptospira interrogans | |
2.3.3.21 | Co2+ | - |
Leptospira interrogans | |
2.3.3.21 | Co2+ | enzymatic activity of LiCMS in the absence and presence of different metal ions. Co2+ is an activator | Leptospira interrogans | |
2.3.3.21 | Cu2+ | enzymatic activity of LiCMS in the absence and presence of different metal ions. Cu2+ is an inhibitor | Leptospira interrogans | |
2.3.3.21 | K+ | - |
Leptospira interrogans | |
2.3.3.21 | 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 | |
2.3.3.21 | Li+ | - |
Leptospira interrogans | |
2.3.3.21 | Mg2+ | - |
Leptospira interrogans | |
2.3.3.21 | Mg2+ | enzymatic activity of LiCMS in the absence and presence of different metal ions. Mg2+ is an activator | Leptospira interrogans | |
2.3.3.21 | Mn2+ | - |
Leptospira interrogans | |
2.3.3.21 | 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 | |
2.3.3.21 | Na+ | - |
Leptospira interrogans | |
2.3.3.21 | NH4+ | - |
Leptospira interrogans | |
2.3.3.21 | NH4+ | can act as a co-activator in the presence of Mn2+ | Leptospira interrogans | |
2.3.3.21 | Ni2+ | - |
Leptospira interrogans | |
2.3.3.21 | Ni2+ | enzymatic activity of LiCMS in the absence and presence of different metal ions. Ni2+ is an activator | Leptospira interrogans | |
2.3.3.21 | Zn2+ | enzymatic activity of LiCMS in the absence and presence of different metal ions. Zn2+ is an inhibitor | Leptospira interrogans |
EC Number | Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|---|
2.3.3.21 | 14000 | - |
corresponds to the C-terminal regulatory domain of LiCMS, SDS-PAGE | Leptospira interrogans |
2.3.3.21 | 33000 | - |
corresponds to the N-terminal catalytic domain of LiCMS, SDS-PAGE | Leptospira interrogans |
2.3.3.21 | 56000 | - |
determined by SDS-PAGE | Leptospira interrogans |
EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
2.3.3.21 | (2S)-2-hydroxy-2-methylbutanedioate | Leptospira interrogans | - |
acetate + pyruvate | - |
r | |
2.3.3.21 | acetyl-CoA + pyruvate + H2O | Leptospira interrogans | - |
CoA + (2R)-2-hydroxy-2-methylbutanedioate | - |
? |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
2.3.3.21 | Leptospira interrogans | - |
- |
- |
EC Number | Purification (Comment) | Organism |
---|---|---|
2.3.3.21 | affinity chromatography using a Ni2+-NTA (Ni2+-nitrilotriacetate) Superflow column | Leptospira interrogans |
2.3.3.21 | 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 |
2.3.3.21 | using a Ni2+-NTA Superflow column and an anion-exchange Q-column, the tag is removed by cleavage with thrombin | Leptospira interrogans |
EC Number | Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
---|---|---|---|---|
2.3.3.21 | additional information | - |
specific activity for Zn2+ -0.04 micromol/min/mg and -0.13 micromol/min/mg for Cu2+ | Leptospira interrogans |
2.3.3.21 | 0.2 | - |
in the absence of metal ions | Leptospira interrogans |
2.3.3.21 | 0.2 | - |
without metals | Leptospira interrogans |
2.3.3.21 | 0.4 | - |
in the presence of K+ | Leptospira interrogans |
2.3.3.21 | 0.4 | - |
with K+ | Leptospira interrogans |
2.3.3.21 | 1.1 | - |
in the presence of Ni2+ | Leptospira interrogans |
2.3.3.21 | 1.1 | - |
with Ni2+ | Leptospira interrogans |
2.3.3.21 | 1.2 | - |
with Mg2+ | Leptospira interrogans |
2.3.3.21 | 1.2 | - |
in the presence of Mg2+ | Leptospira interrogans |
2.3.3.21 | 2.2 | - |
in the presence of Ca2+ | Leptospira interrogans |
2.3.3.21 | 2.2 | - |
with Ca2+ | Leptospira interrogans |
2.3.3.21 | 2.5 | - |
in the presence of Co2+ | Leptospira interrogans |
2.3.3.21 | 2.5 | - |
with Co2+ | Leptospira interrogans |
2.3.3.21 | 6.1 | - |
in the presence of Mn2+ and Li+ | Leptospira interrogans |
2.3.3.21 | 6.1 | - |
with Li+ | Leptospira interrogans |
2.3.3.21 | 6.2 | - |
with Mn2+ | Leptospira interrogans |
2.3.3.21 | 6.2 | - |
in the presence of Mn2+ | Leptospira interrogans |
2.3.3.21 | 6.5 | - |
in the presence of Mn2+ and Na+ | Leptospira interrogans |
2.3.3.21 | 6.5 | - |
with Na+ | Leptospira interrogans |
2.3.3.21 | 7.1 | - |
with Mn2+ | Leptospira interrogans |
2.3.3.21 | 7.1 | - |
in the presence of Mn2+ | Leptospira interrogans |
2.3.3.21 | 9 | - |
in the presence of Mn2+ and NH4+ | Leptospira interrogans |
2.3.3.21 | 9 | - |
with NH4+ | Leptospira interrogans |
2.3.3.21 | 9.4 | - |
in the presence of Mn2+ and K+ | Leptospira interrogans |
2.3.3.21 | 9.4 | - |
with K+ | Leptospira interrogans |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
2.3.3.21 | (2S)-2-hydroxy-2-methylbutanedioate | - |
Leptospira interrogans | acetate + pyruvate | - |
r | |
2.3.3.21 | acetyl-CoA + 2-oxobutyrate + H2O | - |
Leptospira interrogans | ? | - |
? | |
2.3.3.21 | acetyl-CoA + 2-oxoisovalerate + H2O | - |
Leptospira interrogans | ? | - |
? | |
2.3.3.21 | acetyl-CoA + glyoxylate + H2O | - |
Leptospira interrogans | ? | - |
? | |
2.3.3.21 | acetyl-CoA + pyruvate + H2O | - |
Leptospira interrogans | CoA + (2R)-2-hydroxy-2-methylbutanedioate | - |
? | |
2.3.3.21 | acetyl-CoA + pyruvate + H2O | - |
Leptospira interrogans | CoA + (R)-citramalate | - |
? | |
2.3.3.21 | acetyl-CoA + pyruvate + H2O | - |
Leptospira interrogans | (2S)-2-hydroxy-2-methylbutanedioate + CoA | - |
r | |
2.3.3.21 | 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 | ? | - |
? |
EC Number | Subunits | Comment | Organism |
---|---|---|---|
2.3.3.21 | 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 |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
2.3.3.21 | citramalate lyase | - |
Leptospira interrogans |
2.3.3.21 | citramalate synthase | - |
Leptospira interrogans |
2.3.3.21 | LiCMS | - |
Leptospira interrogans |
EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|---|
2.3.3.21 | 37 | - |
activity assay | Leptospira interrogans |
2.3.3.21 | 37 | - |
enzymatic activity assay | Leptospira interrogans |
EC Number | Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
2.3.3.21 | 0.005 | - |
glyoxylate | Y144L mutant | Leptospira interrogans | |
2.3.3.21 | 0.005 | - |
2-oxobutyrate | Y144L mutant | Leptospira interrogans | |
2.3.3.21 | 0.014 | - |
2-oxobutyrate | L81V mutant | Leptospira interrogans | |
2.3.3.21 | 0.017 | - |
acetyl-CoA | Y144L mutant | Leptospira interrogans | |
2.3.3.21 | 0.017 | - |
acetyl-CoA | mutant Y144L, kinetic data for the substrate-binding site of LiCMS | Leptospira interrogans | |
2.3.3.21 | 0.018 | - |
2-oxoisovalerate | L81A mutant | Leptospira interrogans | |
2.3.3.21 | 0.023 | - |
2-oxoisovalerate | Y144L mutant | Leptospira interrogans | |
2.3.3.21 | 0.03 | - |
2-oxobutyrate | L104V mutant | Leptospira interrogans | |
2.3.3.21 | 0.03 | - |
2-oxoisovalerate | L104V mutant | Leptospira interrogans | |
2.3.3.21 | 0.03 | - |
glyoxylate | Y144V mutant | Leptospira interrogans | |
2.3.3.21 | 0.05 | - |
2-oxobutyrate | L81A mutant | Leptospira interrogans | |
2.3.3.21 | 0.062 | - |
2-oxoisovalerate | Y144V mutant | Leptospira interrogans | |
2.3.3.21 | 0.09 | - |
2-oxobutyrate | wild-type | Leptospira interrogans | |
2.3.3.21 | 0.09 | - |
2-oxobutyrate | wild type LiCMS | Leptospira interrogans | |
2.3.3.21 | 0.12 | - |
pyruvate | Y144L mutant | Leptospira interrogans | |
2.3.3.21 | 0.12 | - |
pyruvate | mutant Y144L, kinetic data for the substrate-binding site of LiCMS | Leptospira interrogans | |
2.3.3.21 | 0.19 | - |
glyoxylate | L81A mutant | Leptospira interrogans | |
2.3.3.21 | 0.21 | - |
glyoxylate | L81V mutant | Leptospira interrogans | |
2.3.3.21 | 0.32 | - |
pyruvate | D304A mutant | Leptospira interrogans | |
2.3.3.21 | 0.32 | - |
pyruvate | mutant D304A, kinetic data for the C-terminal region of LiCMS | Leptospira interrogans | |
2.3.3.21 | 0.4 | - |
pyruvate | LiCMSN, N-terminal domain of LiCMS | Leptospira interrogans | |
2.3.3.21 | 0.4 | - |
pyruvate | LiCMSN mutant | Leptospira interrogans | |
2.3.3.21 | 0.4 | - |
pyruvate | LiCMSN, kinetic data for the catalytic reaction of the active site of LiCMS | Leptospira interrogans | |
2.3.3.21 | 0.51 | - |
glyoxylate | wild-type | Leptospira interrogans | |
2.3.3.21 | 0.51 | - |
glyoxylate | wild type LiCMS | Leptospira interrogans | |
2.3.3.21 | 0.58 | - |
pyruvate | L81A mutant | Leptospira interrogans | |
2.3.3.21 | 0.58 | - |
pyruvate | mutant L81A, kinetic data for the substrate-binding site of LiCMS | Leptospira interrogans | |
2.3.3.21 | 0.6 | - |
glyoxylate | L104V mutant | Leptospira interrogans | |
2.3.3.21 | 0.6 | - |
acetyl-CoA | Y144V mutant | Leptospira interrogans | |
2.3.3.21 | 0.6 | - |
acetyl-CoA | mutant Y144V, kinetic data for the substrate-binding site of LiCMS | Leptospira interrogans | |
2.3.3.21 | 0.62 | - |
acetyl-CoA | D304A mutant | Leptospira interrogans | |
2.3.3.21 | 0.62 | - |
2-oxobutyrate | Y144V mutant | Leptospira interrogans | |
2.3.3.21 | 0.62 | - |
acetyl-CoA | mutant D304A, kinetic data for the C-terminal region of LiCMS | Leptospira interrogans | |
2.3.3.21 | 0.7 | - |
acetyl-CoA | L81A mutant | Leptospira interrogans | |
2.3.3.21 | 0.7 | - |
acetyl-CoA | mutant L81A, kinetic data for the substrate-binding site of LiCMS | Leptospira interrogans | |
2.3.3.21 | 0.9 | - |
pyruvate | L81V mutant | Leptospira interrogans | |
2.3.3.21 | 0.9 | - |
pyruvate | mutant L81V, kinetic data for the substrate-binding site of LiCMS | Leptospira interrogans | |
2.3.3.21 | 1.1 | - |
acetyl-CoA | L81V mutant | Leptospira interrogans | |
2.3.3.21 | 1.1 | - |
acetyl-CoA | LiCMSN, N-terminal domain of LiCMS | Leptospira interrogans | |
2.3.3.21 | 1.1 | - |
acetyl-CoA | LiCMSN mutant | Leptospira interrogans | |
2.3.3.21 | 1.1 | - |
acetyl-CoA | LiCMSN, kinetic data for the catalytic reaction of the active site of LiCMS | Leptospira interrogans | |
2.3.3.21 | 1.1 | - |
acetyl-CoA | mutant L81V, kinetic data for the substrate-binding site of LiCMS | Leptospira interrogans | |
2.3.3.21 | 1.7 | - |
acetyl-CoA | L311A mutant | Leptospira interrogans | |
2.3.3.21 | 1.7 | - |
pyruvate | L311A mutant | Leptospira interrogans | |
2.3.3.21 | 1.7 | - |
pyruvate | Y144V mutant | Leptospira interrogans | |
2.3.3.21 | 1.7 | - |
acetyl-CoA | mutant L311A, kinetic data for the C-terminal region of LiCMS | Leptospira interrogans | |
2.3.3.21 | 1.7 | - |
pyruvate | mutant L311A, kinetic data for the C-terminal region of LiCMS | Leptospira interrogans | |
2.3.3.21 | 1.7 | - |
pyruvate | mutant Y144V, kinetic data for the substrate-binding site of LiCMS | Leptospira interrogans | |
2.3.3.21 | 1.9 | - |
pyruvate | D17N mutant | Leptospira interrogans | |
2.3.3.21 | 1.9 | - |
pyruvate | mutant D17N, kinetic data for the catalytic reaction of the active site of LiCMS | Leptospira interrogans | |
2.3.3.21 | 2.1 | - |
acetyl-CoA | E146D mutant | Leptospira interrogans | |
2.3.3.21 | 2.1 | - |
acetyl-CoA | mutant E146D, kinetic data for the catalytic reaction of the active site of LiCMS | Leptospira interrogans | |
2.3.3.21 | 2.4 | - |
acetyl-CoA | E146Q mutant | Leptospira interrogans | |
2.3.3.21 | 2.4 | - |
acetyl-CoA | mutant E146Q, kinetic data for the catalytic reaction of the active site of LiCMS | Leptospira interrogans | |
2.3.3.21 | 2.7 | - |
pyruvate | L104V mutant | Leptospira interrogans | |
2.3.3.21 | 2.7 | - |
pyruvate | mutant L104V, kinetic data for the substrate-binding site of LiCMS | Leptospira interrogans | |
2.3.3.21 | 2.9 | - |
pyruvate | D17A mutant | Leptospira interrogans | |
2.3.3.21 | 2.9 | - |
pyruvate | mutant D17A, kinetic data for the catalytic reaction of the active site of LiCMS | Leptospira interrogans | |
2.3.3.21 | 3.8 | - |
pyruvate | N310A mutant | Leptospira interrogans | |
2.3.3.21 | 3.8 | - |
pyruvate | mutant N310A, kinetic data for the C-terminal region of LiCMS | Leptospira interrogans | |
2.3.3.21 | 3.9 | - |
acetyl-CoA | L104V mutant | Leptospira interrogans | |
2.3.3.21 | 3.9 | - |
acetyl-CoA | mutant L104V, kinetic data for the substrate-binding site of LiCMS | Leptospira interrogans | |
2.3.3.21 | 4.9 | - |
pyruvate | T179A mutant | Leptospira interrogans | |
2.3.3.21 | 4.9 | - |
pyruvate | mutant T179A, kinetic data for the catalytic reaction of the active site of LiCMS | Leptospira interrogans | |
2.3.3.21 | 5.9 | - |
acetyl-CoA | N310A mutant | Leptospira interrogans | |
2.3.3.21 | 5.9 | - |
acetyl-CoA | mutant N310A, kinetic data for the C-terminal region of LiCMS | Leptospira interrogans | |
2.3.3.21 | 8.5 | - |
acetyl-CoA | R16K/R16Q mutant | Leptospira interrogans | |
2.3.3.21 | 8.5 | - |
acetyl-CoA | F83A mutant | Leptospira interrogans | |
2.3.3.21 | 8.5 | - |
acetyl-CoA | mutant F83A, kinetic data for the catalytic reaction of the active site of LiCMS | Leptospira interrogans | |
2.3.3.21 | 9.1 | - |
pyruvate | wild type LiCMS | Leptospira interrogans | |
2.3.3.21 | 9.1 | - |
pyruvate | wild type, kinetic data for the C-terminal region of LiCMS | Leptospira interrogans | |
2.3.3.21 | 9.1 | - |
pyruvate | wild type, kinetic data for the substrate-binding site of LiCMS | Leptospira interrogans | |
2.3.3.21 | 9.13 | - |
pyruvate | wild-type | Leptospira interrogans | |
2.3.3.21 | 9.13 | - |
pyruvate | wild type LiCMS | Leptospira interrogans | |
2.3.3.21 | 9.13 | - |
pyruvate | wild type, kinetic data for the catalytic reaction of the active site of LiCMS | Leptospira interrogans | |
2.3.3.21 | 10.3 | - |
acetyl-CoA | wild-type | Leptospira interrogans | |
2.3.3.21 | 10.3 | - |
acetyl-CoA | wild type LiCMS | Leptospira interrogans | |
2.3.3.21 | 10.3 | - |
acetyl-CoA | wild type, kinetic data for the C-terminal region of LiCMS | Leptospira interrogans | |
2.3.3.21 | 10.3 | - |
acetyl-CoA | wild type, kinetic data for the catalytic reaction of the active site of LiCMS | Leptospira interrogans | |
2.3.3.21 | 10.3 | - |
acetyl-CoA | wild type, kinetic data for the substrate-binding site of LiCMS | Leptospira interrogans |
EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|---|
2.3.3.21 | 7.7 | - |
activity assay | Leptospira interrogans |
2.3.3.21 | 7.7 | - |
enzymatic activity assay | Leptospira interrogans |