Cloned (Comment) | Organism |
---|---|
expressed in Pseudomonas syringae pv. syringae FF5 as a FLAG-tagged protein | Pseudomonas syringae |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.04 | - |
L-allo-isoleucine | pH 7.5, 25°C, the assay measures the release of diphosphate by means of a coupled enzyme system in which diphosphate drives the reduction of NAD+ to NADH | Pseudomonas syringae | |
0.5 | - |
L-isoleucine | pH 7.5, 25°C, the assay measures the release of diphosphate by means of a coupled enzyme system in which diphosphate drives the reduction of NAD+ to NADH | Pseudomonas syringae | |
1.2 | - |
L-valine | pH 7.5, 25°C, the assay measures the release of diphosphate by means of a coupled enzyme system in which diphosphate drives the reduction of NAD+ to NADH | Pseudomonas syringae | |
1.5 | - |
L-leucine | pH 7.5, 25°C, the assay measures the release of diphosphate by means of a coupled enzyme system in which diphosphate drives the reduction of NAD+ to NADH | Pseudomonas syringae |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
ATP + L-allo-isoleucine + [CmaA -protein-T-domain]-4'-phosphopantetheine | Pseudomonas syringae | the didomain protein contains an adenylation domain (A domain) and a thiolation domain (T domain). It catalyzes the adenylation of L-allo-isoleucine and the attachment of L-allo-isoleucine to the CmaA T domain. The enzyme-bound L-allo-isoleucine serves as the substrate for the later stages of the biosdynthesis of the toxin coronatine. This toxin mimics the plant hormone jasmonic acid isoleucine and promotes opening of stomata for bacterial entry, bacterial growth in the apoplast, systemic susceptibility, and disease | AMP + diphosphate + S-L-allo-isoleucyl-[CmaA-protein-T-domain]-4'-phosphopantetheine | - |
? | |
ATP + L-allo-isoleucine + [CmaA -protein-T-domain]-4'-phosphopantetheine | Pseudomonas syringae pv. glycinea PG4180 | the didomain protein contains an adenylation domain (A domain) and a thiolation domain (T domain). It catalyzes the adenylation of L-allo-isoleucine and the attachment of L-allo-isoleucine to the CmaA T domain. The enzyme-bound L-allo-isoleucine serves as the substrate for the later stages of the biosdynthesis of the toxin coronatine. This toxin mimics the plant hormone jasmonic acid isoleucine and promotes opening of stomata for bacterial entry, bacterial growth in the apoplast, systemic susceptibility, and disease | AMP + diphosphate + S-L-allo-isoleucyl-[CmaA-protein-T-domain]-4'-phosphopantetheine | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Pseudomonas syringae | Q6TNA5 | - |
- |
Pseudomonas syringae pv. glycinea PG4180 | Q6TNA5 | - |
- |
Purification (Comment) | Organism |
---|---|
- |
Pseudomonas syringae |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
ATP + L-allo-isoleucine + [CmaA -protein-T-domain]-4'-phosphopantetheine | the didomain protein contains an adenylation domain (A domain) and a thiolation domain (T domain). It catalyzes the adenylation of L-allo-isoleucine and the attachment of L-allo-isoleucine to the CmaA T domain. The enzyme-bound L-allo-isoleucine serves as the substrate for the later stages of the biosdynthesis of the toxin coronatine. This toxin mimics the plant hormone jasmonic acid isoleucine and promotes opening of stomata for bacterial entry, bacterial growth in the apoplast, systemic susceptibility, and disease | Pseudomonas syringae | AMP + diphosphate + S-L-allo-isoleucyl-[CmaA-protein-T-domain]-4'-phosphopantetheine | - |
? | |
ATP + L-allo-isoleucine + [CmaA -protein-T-domain]-4'-phosphopantetheine | the didomain protein contains an adenylation domain (A domain) and a thiolation domain (T domain). It catalyzes the adenylation of L-allo-isoleucine and the attachment of L-allo-isoleucine to the CmaA T domain. The enzyme-bound L-allo-isoleucine serves as the substrate for the later stages of the biosdynthesis of the toxin coronatine. This toxin mimics the plant hormone jasmonic acid isoleucine and promotes opening of stomata for bacterial entry, bacterial growth in the apoplast, systemic susceptibility, and disease | Pseudomonas syringae pv. glycinea PG4180 | AMP + diphosphate + S-L-allo-isoleucyl-[CmaA-protein-T-domain]-4'-phosphopantetheine | - |
? | |
ATP + L-allo-isoleucine + [CmaA-protein-T-domain]-4'-phosphopantetheine | the enzyme catalyzes the adenylation of L-isoleucine, L-leucine and L-valine with about 40% of the activity compared to L-allo-isoleucine | Pseudomonas syringae | AMP + diphosphate + S-L-allo-isoleucyl-[CmaA-protein-T-domain]-4'-phosphopantetheine | - |
? | |
ATP + L-allo-isoleucine + [CmaA-protein-T-domain]-4'-phosphopantetheine | the enzyme catalyzes the adenylation of L-isoleucine, L-leucine and L-valine with about 40% of the activity compared to L-allo-isoleucine | Pseudomonas syringae pv. glycinea PG4180 | AMP + diphosphate + S-L-allo-isoleucyl-[CmaA-protein-T-domain]-4'-phosphopantetheine | - |
? | |
ATP + L-isoleucine + [CmaA-protein-T-domain]-4'-phosphopantetheine | the enzyme catalyzes the adenylation of L-isoleucine, L-leucine and L-valine with about 40% of the activity compared to L-allo-isoleucine | Pseudomonas syringae | AMP + diphosphate + S-L-isoleucyl-[CmaA-protein-T-domain]-4'-phosphopantetheine | - |
? | |
ATP + L-isoleucine + [CmaA-protein-T-domain]-4'-phosphopantetheine | the enzyme catalyzes the adenylation of L-isoleucine, L-leucine and L-valine with about 40% of the activity compared to L-allo-isoleucine | Pseudomonas syringae pv. glycinea PG4180 | AMP + diphosphate + S-L-isoleucyl-[CmaA-protein-T-domain]-4'-phosphopantetheine | - |
? | |
ATP + L-leucine + [CmaA-protein-T-domain]-4'-phosphopantetheine | the enzyme catalyzes the adenylation of L-isoleucine, L-leucine and L-valine with about 40% of the activity compared to L-allo-isoleucine | Pseudomonas syringae | AMP + diphosphate + S-L-leucyl-[CmaA-protein-T-domain]-4'-phosphopantetheine | - |
? | |
ATP + L-leucine + [CmaA-protein-T-domain]-4'-phosphopantetheine | the enzyme catalyzes the adenylation of L-isoleucine, L-leucine and L-valine with about 40% of the activity compared to L-allo-isoleucine | Pseudomonas syringae pv. glycinea PG4180 | AMP + diphosphate + S-L-leucyl-[CmaA-protein-T-domain]-4'-phosphopantetheine | - |
? | |
ATP + L-valine + [CmaA-protein-T-domain]-4'-phosphopantetheine | the enzyme catalyzes the adenylation of L-isoleucine, L-leucine and L-valine with about 40% of the activity compared to L-allo-isoleucine | Pseudomonas syringae | AMP + diphosphate + S-L-valyl-[CmaA-protein-T-domain]-4'-phosphopantetheine | - |
? | |
ATP + L-valine + [CmaA-protein-T-domain]-4'-phosphopantetheine | the enzyme catalyzes the adenylation of L-isoleucine, L-leucine and L-valine with about 40% of the activity compared to L-allo-isoleucine | Pseudomonas syringae pv. glycinea PG4180 | AMP + diphosphate + S-L-valyl-[CmaA-protein-T-domain]-4'-phosphopantetheine | - |
? |
Subunits | Comment | Organism |
---|---|---|
dimer | - |
Pseudomonas syringae |
Synonyms | Comment | Organism |
---|---|---|
CmaA | - |
Pseudomonas syringae |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
25 | - |
assay at | Pseudomonas syringae |
Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.0015 | - |
L-allo-isoleucine | pH 7.5, 25°C, the assay measures the release of diphosphate by means of a coupled enzyme system in which diphosphate drives the reduction of NAD+ to NADH | Pseudomonas syringae | |
0.012 | - |
L-isoleucine | pH 7.5, 25°C, the assay measures the release of diphosphate by means of a coupled enzyme system in which diphosphate drives the reduction of NAD+ to NADH | Pseudomonas syringae | |
0.023 | - |
L-valine | pH 7.5, 25°C, the assay measures the release of diphosphate by means of a coupled enzyme system in which diphosphate drives the reduction of NAD+ to NADH | Pseudomonas syringae | |
0.03 | - |
L-leucine | pH 7.5, 25°C, the assay measures the release of diphosphate by means of a coupled enzyme system in which diphosphate drives the reduction of NAD+ to NADH | Pseudomonas syringae |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
7.5 | - |
assay at | Pseudomonas syringae |
General Information | Comment | Organism |
---|---|---|
physiological function | the enzyme is involved in the biosynthesis of the toxin coronatine. This toxin mimics the plant hormone jasmonic acid isoleucine and promotes opening of stomata for bacterial entry, bacterial growth in the apoplast, systemic susceptibility, and disease symptoms | Pseudomonas syringae |
kcat/KM Value [1/mMs-1] | kcat/KM Value Maximum [1/mMs-1] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.019 | - |
L-valine | pH 7.5, 25°C, the assay measures the release of diphosphate by means of a coupled enzyme system in which diphosphate drives the reduction of NAD+ to NADH | Pseudomonas syringae | |
0.02 | - |
L-leucine | pH 7.5, 25°C, the assay measures the release of diphosphate by means of a coupled enzyme system in which diphosphate drives the reduction of NAD+ to NADH | Pseudomonas syringae | |
0.024 | - |
L-isoleucine | pH 7.5, 25°C, the assay measures the release of diphosphate by means of a coupled enzyme system in which diphosphate drives the reduction of NAD+ to NADH | Pseudomonas syringae | |
0.0375 | - |
L-allo-isoleucine | pH 7.5, 25°C, the assay measures the release of diphosphate by means of a coupled enzyme system in which diphosphate drives the reduction of NAD+ to NADH | Pseudomonas syringae |