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Literature summary extracted from

  • Couch, R.; O'Connor, S.E.; Seidle, H.; Walsh, C.T.; Parry, R.
    Characterization of CmaA, an adenylation-thiolation didomain enzyme involved in the biosynthesis of coronatine (2004), J. Bacteriol., 186, 35-42.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
6.2.1.46 expressed in Pseudomonas syringae pv. syringae FF5 as a FLAG-tagged protein Pseudomonas syringae

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
6.2.1.46 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
6.2.1.46 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
6.2.1.46 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
6.2.1.46 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/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
6.2.1.46 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
-
 ?
6.2.1.46 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

EC Number Organism UniProt Comment Textmining
6.2.1.46 Pseudomonas syringae Q6TNA5
-
-
6.2.1.46 Pseudomonas syringae pv. glycinea PG4180 Q6TNA5
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
6.2.1.46
-
 Pseudomonas syringae

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
6.2.1.46 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
-
 ?
6.2.1.46 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
-
 ?
6.2.1.46 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
-
 ?
6.2.1.46 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
-
 ?
6.2.1.46 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
-
 ?
6.2.1.46 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
-
 ?
6.2.1.46 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
-
 ?
6.2.1.46 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
-
 ?
6.2.1.46 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
-
 ?
6.2.1.46 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

EC Number Subunits Comment Organism
6.2.1.46 dimer
-
 Pseudomonas syringae

Synonyms

EC Number Synonyms Comment Organism
6.2.1.46 CmaA
-
 Pseudomonas syringae

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
6.2.1.46 25
-
 assay at Pseudomonas syringae

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
6.2.1.46 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
6.2.1.46 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
6.2.1.46 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
6.2.1.46 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

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
6.2.1.46 7.5
-
 assay at Pseudomonas syringae

General Information

EC Number General Information Comment Organism
6.2.1.46 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 [mM/s]

EC Number kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
6.2.1.46 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
6.2.1.46 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
6.2.1.46 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
6.2.1.46 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