Cloned (Comment) | Organism |
---|---|
sequence comparisons | Yersinia pestis |
sequence comparisons | Escherichia coli |
Protein Variants | Comment | Organism |
---|---|---|
K190A | inactive mutant | Escherichia coli |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
(4R,5R)-5-(carboxymethoxy)-4-hydroxycyclohex-1-ene-1-carboxylic acid | - |
Escherichia coli | |
(4R,5R)-5-[(1-carboxyethenyl)oxy]-4-hydroxycyclohex-1-ene-1-carboxylic acid | inhibition of isochorismate synthase activity and salicylate synthase activity | Escherichia coli | |
(4R,5R)-5-[(1-carboxyethenyl)oxy]-4-hydroxycyclohex-1-ene-1-carboxylic acid | - |
Mycobacterium tuberculosis | |
(4R,5R)-5-[(1-carboxyethenyl)oxy]-4-hydroxycyclohex-1-ene-1-carboxylic acid | - |
Pseudomonas aeruginosa | |
(4R,5R)-5-[(1-carboxyethenyl)oxy]-4-hydroxycyclohex-1-ene-1-carboxylic acid | - |
Yersinia enterocolitica | |
(4R,5R)-5-[(1-carboxyethenyl)oxy]-4-hydroxycyclohex-1-ene-1-carboxylic acid | - |
Yersinia pestis | |
(4R,5R)-5-[(1R)-1-carboxyethoxy]-4-hydroxycyclohex-1-ene-1-carboxylic acid | - |
Escherichia coli | |
(4R,5R)-5-[(1S)-1-carboxyethoxy]-4-hydroxycyclohex-1-ene-1-carboxylic acid | - |
Escherichia coli | |
(4R,5R)-5-[(2-carboxyprop-2-en-1-yl)oxy]-4-hydroxycyclohex-1-ene-1-carboxylic acid | - |
Escherichia coli | |
(4R,5R,6S)-6-amino-5-[(1-carboxyethenyl)oxy]-4-hydroxycyclohex-1-ene-1-carboxylic acid | - |
Escherichia coli | |
(4R,5R,6S)-6-amino-5-[(1-carboxyethenyl)oxy]-4-hydroxycyclohex-1-ene-1-carboxylic acid | - |
Pseudomonas aeruginosa | |
(4R,5S,6S)-4-amino-5-[(1-carboxyethenyl)oxy]-6-hydroxycyclohex-1-ene-1-carboxylic acid | - |
Escherichia coli | |
(4R,5S,6S)-4-amino-5-[(1-carboxyethenyl)oxy]-6-hydroxycyclohex-1-ene-1-carboxylic acid | - |
Pseudomonas aeruginosa | |
(4R,5S,6S)-5-[(1-carboxyethenyl)oxy]-4,6-dihydroxycyclohex-1-ene-1-carboxylic acid | - |
Escherichia coli | |
(4R,5S,6S)-5-[(1-carboxyethenyl)oxy]-4,6-dihydroxycyclohex-1-ene-1-carboxylic acid | - |
Pseudomonas aeruginosa | |
additional information | inhibitor structure-function relationship and molecular docking | Escherichia coli | |
additional information | inhibitor structure-function realtionship and molecular docking | Mycobacterium tuberculosis | |
additional information | inhibitor structure-function relationship and molecular docking | Pseudomonas aeruginosa | |
additional information | inhibitor structure-function relationship and molecular docking | Yersinia enterocolitica | |
additional information | inhibitor structure-function relationship and molecular docking | Yersinia pestis |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Mg2+ | required | Yersinia pestis | |
Mg2+ | required | Yersinia enterocolitica | |
Mg2+ | required | Mycobacterium tuberculosis | |
Mg2+ | strongly dependent on, magnesium ions interact with chorismate in the active site, forming a magnesium-coordinated transition state during the reaction | Escherichia coli | |
Mg2+ | strongly dependent on, magnesium ions interact with chorismate in the active site, forming a magnesium-coordinated transition state during the reaction | Pseudomonas aeruginosa |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
Chorismate | Yersinia pestis | - |
Isochorismate | - |
r | |
Chorismate | Yersinia enterocolitica | - |
Isochorismate | - |
r | |
Chorismate | Mycobacterium tuberculosis | - |
Isochorismate | - |
r | |
Chorismate | Mycobacterium tuberculosis ATCC 25618 | - |
Isochorismate | - |
r | |
isochorismate | Escherichia coli | - |
chorismate | - |
r | |
isochorismate | Pseudomonas aeruginosa | - |
chorismate | - |
r |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Escherichia coli | P38051 | - |
- |
Mycobacterium tuberculosis | P9WFX1 | - |
- |
no activity in Homo sapiens | - |
- |
- |
Pseudomonas aeruginosa | Q51508 | - |
- |
Yersinia enterocolitica | - |
- |
- |
Yersinia pestis | - |
- |
- |
Reaction | Comment | Organism | Reaction ID |
---|---|---|---|
chorismate = isochorismate | isochorismate synthase (IS) performs a 1,5-displacement mechanism during the chorismate conversion to intermediates through the use of a nucleophile, which is water in the case of IS, but might also be possible with ammonia. The hydroxyl group in the isochorismate is generated from water and not through an intramolecular rearrangement | Escherichia coli | |
chorismate = isochorismate | isochorismate synthase performs a 1,5-displacement mechanism during the chorismate conversion to intermediates through the use of a nucleophile, which is water in the case of isochorismate synthase, but might also be possible with ammonia. The hydroxyl group in the isochorismate is generated from water and not through an intramolecular rearrangement | Pseudomonas aeruginosa |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
Chorismate | - |
Yersinia pestis | Isochorismate | - |
r | |
Chorismate | - |
Yersinia enterocolitica | Isochorismate | - |
r | |
Chorismate | - |
Mycobacterium tuberculosis | Isochorismate | - |
r | |
Chorismate | - |
Mycobacterium tuberculosis ATCC 25618 | Isochorismate | - |
r | |
isochorismate | - |
Escherichia coli | chorismate | - |
r | |
isochorismate | - |
Pseudomonas aeruginosa | chorismate | - |
r | |
additional information | the bifunctional salicylate synthase converts chorismate into salicylate through a two-step reaction, exhibiting both isochorismate synthase (EC 5.4.4.2) and isochorismate lyase (EC 4.2.99.21) activities | Yersinia pestis | ? | - |
? | |
additional information | the bifunctional salicylate synthase converts chorismate into salicylate through a two-step reaction, exhibiting both isochorismate synthase (EC 5.4.4.2) and isochorismate lyase (EC 4.2.99.21) activities | Yersinia enterocolitica | ? | - |
? | |
additional information | the bifunctional salicylate synthase converts chorismate into salicylate through a two-step reaction, exhibiting both isochorismate synthase (EC 5.4.4.2) and isochorismate lyase (EC 4.2.99.21) activities | Mycobacterium tuberculosis | ? | - |
? | |
additional information | the bifunctional salicylate synthase converts chorismate into salicylate through a two-step reaction, exhibiting both isochorismate synthase (EC 5.4.4.2) and isochorismate lyase (EC 4.2.99.21) activities | Mycobacterium tuberculosis ATCC 25618 | ? | - |
? |
Subunits | Comment | Organism |
---|---|---|
monomer | - |
Escherichia coli |
Synonyms | Comment | Organism |
---|---|---|
MenF | - |
Escherichia coli |
PchA | - |
Pseudomonas aeruginosa |
salicylate biosynthesis isochorismate synthase | UniProt | Pseudomonas aeruginosa |
salicylate synthase | EC 5.4.4.2 and 4.2.99.21 | Yersinia pestis |
salicylate synthase | EC 5.4.4.2 and 4.2.99.21 | Yersinia enterocolitica |
salicylate synthase | EC 5.4.4.2 and 4.2.99.21 | Mycobacterium tuberculosis |
Ki Value [mM] | Ki Value maximum [mM] | Inhibitor | Comment | Organism | Structure |
---|---|---|---|---|---|
0.000053 | - |
(4R,5R,6S)-6-amino-5-[(1-carboxyethenyl)oxy]-4-hydroxycyclohex-1-ene-1-carboxylic acid | pH and temperature not specified in the publication | Escherichia coli | |
0.00036 | - |
(4R,5S,6S)-5-[(1-carboxyethenyl)oxy]-4,6-dihydroxycyclohex-1-ene-1-carboxylic acid | pH and temperature not specified in the publication | Escherichia coli | |
0.00046 | - |
(4R,5S,6S)-4-amino-5-[(1-carboxyethenyl)oxy]-6-hydroxycyclohex-1-ene-1-carboxylic acid | pH and temperature not specified in the publication | Escherichia coli | |
0.03 | - |
(4R,5R)-5-[(1-carboxyethenyl)oxy]-4-hydroxycyclohex-1-ene-1-carboxylic acid | pH and temperature not specified in the publication, inhibition of isochorismate synthase activity | Escherichia coli | |
0.16 | - |
(4R,5R)-5-[(1-carboxyethenyl)oxy]-4-hydroxycyclohex-1-ene-1-carboxylic acid | pH and temperature not specified in the publication, inhibition of salicylate synthase activity | Escherichia coli |
General Information | Comment | Organism |
---|---|---|
metabolism | the first committed step during the biosynthesis of siderophores, which are small molecules capable of chelating iron from the host organism, is the conversion of chorismate into isochorismate by isochorismate synthase (EC 5.4.4.2) and consequently to salicylate by isochorismate pyruvate-lyase (EC 4.2.99.21). Salicylate synthase converts chorismate into salicylate through a two-step reaction | Escherichia coli |
metabolism | the first committed step during the biosynthesis of siderophores, which are small molecules capable of chelating iron from the host organism, is the conversion of chorismate into isochorismate by isochorismate synthase (EC 5.4.4.2) and consequently to salicylate by isochorismate pyruvate-lyase (EC 4.2.99.21). Salicylate synthase converts chorismate into salicylate through a two-step reaction | Pseudomonas aeruginosa |
metabolism | the first committed step during the biosynthesis of siderophores, which are small molecules capable of chelating iron from the host organism, is the conversion of chorismate into isochorismate by isochorismate synthase (EC 5.4.4.2) and consequently to salicylate by isochorismate pyruvate-lyase (EC 4.2.99.21). the bifunctional salicylate synthase converts chorismate into salicylate through a two-step reaction, exhibiting both isochorismate synthase (EC 5.4.4.2) and isochorismate lyase (EC 4.2.99.21) activities | Yersinia pestis |
metabolism | the first committed step during the biosynthesis of siderophores, which are small molecules capable of chelating iron from the host organism, is the conversion of chorismate into isochorismate by isochorismate synthase (EC 5.4.4.2) and consequently to salicylate by isochorismate pyruvate-lyase (EC 4.2.99.21). the bifunctional salicylate synthase converts chorismate into salicylate through a two-step reaction, exhibiting both isochorismate synthase (EC 5.4.4.2) and isochorismate lyase (EC 4.2.99.21) activities | Yersinia enterocolitica |
metabolism | the first committed step during the biosynthesis of siderophores, which are small molecules capable of chelating iron from the host organism, is the conversion of chorismate into isochorismate by isochorismate synthase (EC 5.4.4.2) and consequently to salicylate by isochorismate pyruvate-lyase (EC 4.2.99.21). the bifunctional salicylate synthase converts chorismate into salicylate through a two-step reaction, exhibiting both isochorismate synthase (EC 5.4.4.2) and isochorismate lyase (EC 4.2.99.21) activities | Mycobacterium tuberculosis |
additional information | enzyme three-dimensional structure analysis, the lysine residue, Lys190, might be involved in the activation of water molecules and the subsequent nucleophilic attack on the C2 carbon of chorismate without directly involving the magnesium ion, participation of the Lys residue during the activation of the substrate or nucleophilic agent | Escherichia coli |
additional information | enzyme three-dimensional structure analysis, the lysine residue, Lys190, might be involved in the activation of water molecules and the subsequent nucleophilic attack on the C2 carbon of chorismate without directly involving the magnesium ion, participation of the Lys residue during the activation of the substrate or nucleophilic agent | Pseudomonas aeruginosa |
physiological function | chorismate-utilizing enzymes (CUE) such as chorismate mutase, anthranilate synthase, chorismate pyruvate-lyase, 4-amino-4-deoxychorismate synthase, isochorismate synthase and salicylate synthase are responsible for converting chorismate into various products necessary for the survival of bacteria | Escherichia coli |
physiological function | the enzyme is involved in the biosynthesis of pyochelin. Chorismate-utilizing enzymes (CUE) such as chorismate mutase, anthranilate synthase, chorismate pyruvate-lyase, 4-amino-4-deoxychorismate synthase, isochorismate synthase and salicylate synthase are responsible for converting chorismate into various products necessary for the survival of bacteria | Pseudomonas aeruginosa |
physiological function | the enzyme is involved in the biosynthesis of the siderophore mycobactin. Chorismate-utilizing enzymes (CUE) such as chorismate mutase, anthranilate synthase, chorismate pyruvate-lyase, 4-amino-4-deoxychorismate synthase, isochorismate synthase and salicylate synthase are responsible for converting chorismate into various products necessary for the survival of bacteria | Mycobacterium tuberculosis |
physiological function | the enzyme is involved in the biosynthesis of the siderophore yersiniabactin. Chorismate-utilizing enzymes (CUE) such as chorismate mutase, anthranilate synthase, chorismate pyruvate-lyase, 4-amino-4-deoxychorismate synthase, isochorismate synthase and salicylate synthase are responsible for converting chorismate into various products necessary for the survival of bacteria | Yersinia pestis |
physiological function | the enzyme is involved in the biosynthesis of the siderophore yersiniabactin. Chorismate-utilizing enzymes (CUE) such as chorismate mutase, anthranilate synthase, chorismate pyruvate-lyase, 4-amino-4-deoxychorismate synthase, isochorismate synthase and salicylate synthase are responsible for converting chorismate into various products necessary for the survival of bacteria | Yersinia enterocolitica |