EC number:2.2.1.6
Enzyme
Download| EC Tree |
| 2. Transferases |
| 2.2 Transferring aldehyde or ketonic groups |
| 2.2.1 Transketolases and transaldolases |
| ID: | 2.2.1.6 | ||
|---|---|---|---|
| Description: | Acetolactate synthase. | ||
| Alternative Name: |
Alpha-acetolactate synthetase. Alpha-acetolactate synthase. Alpha-acetohydroxyacid synthase. Alpha-acetohydroxy acid synthetase. Acetolactic synthetase. Acetolactate pyruvate-lyase (carboxylating). Acetohydroxyacid synthase. Acetohydroxy acid synthetase. | ||
| Prosite: | PDOC00166; | ||
| PDB: |
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| Cath: | 1.20.5.740; 3.30.70.1150; 3.30.70.260; 3.40.50.970; 3.40.50.1220; |
3D structure
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External Links
| UniProtKB Enzyme Link: | UniProtKB 2.2.1.6 |
| BRENDA Enzyme Link: | BRENDA 2.2.1.6 |
| KEGG Enzyme Link: | KEGG2.2.1.6 |
| BioCyc Enzyme Link: | BioCyc 2.2.1.6 |
| ExPASy Enzyme Link: | ExPASy2.2.1.6 |
| EC2PDB Enzyme Link: | EC2PDB 2.2.1.6 |
| ExplorEnz Enzyme Link: | ExplorEnz 2.2.1.6 |
| PRIAM enzyme-specific profiles Link: | PRIAM 2.2.1.6 |
| IntEnz Enzyme Link: | IntEnz 2.2.1.6 |
| MEDLINE Enzyme Link: | MEDLINE 2.2.1.6 |
| RHEA:27654 | 2-oxobutanoate + H(+) + pyruvate = (S)-2-ethyl-2-hydroxy-3-oxobutanoate + CO2 |
| RULE(radius=1) | [*:1]-[C;H0;+0:2](-[*:3])=[O;H0;+0:4].[*:5]=[C;H0;+0:6](-[*:7])-[C;H0;+0:8](=[*:9])-[OH;+0:10].[H+;H0:11]>>[*:5]=[C;H0;+0:6](-[*:7])-[C;H0;+0:2](-[*:1])(-[*:3])-[OH;+0:4].[*:9]=[C;H0;+0:8]=[O;H0;+0:10] |
| Reaction |  |
| Core-to-Core | No scaffolds atoms were exchanged as a result of the reaction |
References
| Title | Authors | Date | PubMed ID |
|---|---|---|---|
| The pH 6 acetolactate-forming enzyme from Aerobacter aerogenes. Molecular properties. | Störmer FC, Solberg Y, Hovig T | 1969 Sep | 5823101 |
| The pH 6 acetolactate-forming enzyme from Aerobacter aerogenes. Subunit structure. | Huseby NE, Christensen TB, Olsen BR, Stormer FC | 1971 May 28 | 5560406 |
| Physiological implications of the specificity of acetohydroxy acid synthase isozymes of enteric bacteria. | Barak Z, Chipman DM, Gollop N | 1987 Aug | 3301814 |
| The crystal structures of Klebsiella pneumoniae acetolactate synthase with enzyme-bound cofactor and with an unusual intermediate. | Pang SS, Duggleby RG, Schowen RL, Guddat LW | 2004 Jan 16 | 14557277 |
| RHEA:25249 | H(+) + 2 pyruvate = (2S)-2-acetolactate + CO2 |
| RULE(radius=1) | [*:1]-[C;H0;+0:2](-[*:3])(-[OH;+0:4])-[C;H0;+0:5](=[*:6])-[*:7].[*:8]=[C;H0;+0:9]=[O;H0;+0:10]>>[*:1]-[C;H0;+0:2](-[*:3])=[O;H0;+0:4].[*:8]=[C;H0;+0:9](-[OH;+0:10])-[C;H0;+0:5](=[*:6])-[*:7] |
| Reaction |  |
| Core-to-Core | No scaffolds atoms were exchanged as a result of the reaction |
References
| Title | Authors | Date | PubMed ID |
|---|---|---|---|
| The pH 6 acetolactate-forming enzyme from Aerobacter aerogenes. Molecular properties. | Störmer FC, Solberg Y, Hovig T | 1969 Sep | 5823101 |
| The pH 6 acetolactate-forming enzyme from Aerobacter aerogenes. Subunit structure. | Huseby NE, Christensen TB, Olsen BR, Stormer FC | 1971 May 28 | 5560406 |
| Physiological implications of the specificity of acetohydroxy acid synthase isozymes of enteric bacteria. | Barak Z, Chipman DM, Gollop N | 1987 Aug | 3301814 |
| The crystal structures of Klebsiella pneumoniae acetolactate synthase with enzyme-bound cofactor and with an unusual intermediate. | Pang SS, Duggleby RG, Schowen RL, Guddat LW | 2004 Jan 16 | 14557277 |