EC Number | Cloned (Comment) | Organism |
---|---|---|
4.2.1.144 | expression in Escherichia coli | Amycolatopsis mediterranei |
EC Number | Crystallization (Comment) | Organism |
---|---|---|
4.2.1.144 | in complex with pyridoxal 5'-phosphate and with pyridoxal 5'-phosphate and inhibitor gabaculine. The overall fold of is similar to that of the aspartate aminotransferase family of PLP-dependent enzymes, with a large domain containing a seven-stranded beta-sheet surrounded by alpha-helices and a smaller domain consisting of a four-stranded antiparallel beta-sheet and four alpha-helices. The uninhibited form of the enzyme shows the cofactor covalently linked to residue Lys188 in an internal aldimine linkage. On binding the inhibitor, gabaculine, the internal aldimine linkage is broken, and a covalent bond is observed between the cofactor and inhibitor. The active site is composed of residues from two subunits, indicating that the enzyme is active as a dimer | Amycolatopsis mediterranei |
EC Number | Inhibitors | Comment | Organism | Structure |
---|---|---|---|---|
4.2.1.144 | gabaculine | crystal structure of the complex with enzyme | Amycolatopsis mediterranei |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
4.2.1.144 | Amycolatopsis mediterranei | O52552 | - |
- |
4.2.1.144 | Amycolatopsis mediterranei S699 | O52552 | - |
- |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
4.2.1.144 | 5-amino-5-deoxy-3-dehydroshikimate | - |
Amycolatopsis mediterranei | 3-amino-5-hydroxybenzoate + H2O | - |
? | |
4.2.1.144 | 5-amino-5-deoxy-3-dehydroshikimate | - |
Amycolatopsis mediterranei S699 | 3-amino-5-hydroxybenzoate + H2O | - |
? |
EC Number | Subunits | Comment | Organism |
---|---|---|---|
4.2.1.144 | dimer | crystal structure | Amycolatopsis mediterranei |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
4.2.1.144 | 3-amino-5-hydroxybenzoic acid synthase | - |
Amycolatopsis mediterranei |
4.2.1.144 | AHBA synthase | - |
Amycolatopsis mediterranei |
4.2.1.144 | rifK | - |
Amycolatopsis mediterranei |
EC Number | Cofactor | Comment | Organism | Structure |
---|---|---|---|---|
4.2.1.144 | pyridoxal 5'-phosphate | - |
Amycolatopsis mediterranei |
EC Number | General Information | Comment | Organism |
---|---|---|---|
4.2.1.144 | physiological function | involved in rifamycin B biosynthesis. Starter enzyme for the assembly of the antibiotics' polyketide backbone | Amycolatopsis mediterranei |