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Literature summary extracted from

  • Eads, J.C.; Beeby, M.; Scapin, G.; Yu, T.W.; Floss, H.G.
    Crystal structure of 3-amino-5-hydroxybenzoic acid (AHBA) synthase (1999), Biochemistry, 38, 9840-9849.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
4.2.1.144 expression in Escherichia coli Amycolatopsis mediterranei

Crystallization (Commentary)

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

Inhibitors

EC Number Inhibitors Comment Organism Structure
4.2.1.144 gabaculine crystal structure of the complex with enzyme Amycolatopsis mediterranei

Organism

EC Number Organism UniProt Comment Textmining
4.2.1.144 Amycolatopsis mediterranei O52552
-
-
4.2.1.144 Amycolatopsis mediterranei S699 O52552
-
-

Substrates and Products (Substrate)

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
-
 ?

Subunits

EC Number Subunits Comment Organism
4.2.1.144 dimer crystal structure Amycolatopsis mediterranei

Synonyms

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

Cofactor

EC Number Cofactor Comment Organism Structure
4.2.1.144 pyridoxal 5'-phosphate
-
 Amycolatopsis mediterranei

General Information

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