Literature summary for 4.2.1.144 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.

Search for more literature for 4.2.1.144

Cloned(Commentary)

Cloned (Comment)	Organism
expression in Escherichia coli	Amycolatopsis mediterranei

Crystallization (Commentary)

Crystallization (Comment)	Organism
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

Crystallization (Comment)

Organism

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

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

Organism

Organism	UniProt	Comment	Textmining
Amycolatopsis mediterranei	O52552	-	-
Amycolatopsis mediterranei S699	O52552	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
5-amino-5-deoxy-3-dehydroshikimate	-	Amycolatopsis mediterranei	3-amino-5-hydroxybenzoate + H2O	-	?
5-amino-5-deoxy-3-dehydroshikimate	-	Amycolatopsis mediterranei S699	3-amino-5-hydroxybenzoate + H2O	-	?

Subunits

Subunits	Comment	Organism
dimer	crystal structure	Amycolatopsis mediterranei

Synonyms

Synonyms	Comment	Organism
3-amino-5-hydroxybenzoic acid synthase	-	Amycolatopsis mediterranei
AHBA synthase	-	Amycolatopsis mediterranei
rifK	-	Amycolatopsis mediterranei

Cofactor

Cofactor	Comment	Organism	Structure
pyridoxal 5'-phosphate	-	Amycolatopsis mediterranei

General Information

General Information	Comment	Organism
physiological function	involved in rifamycin B biosynthesis. Starter enzyme for the assembly of the antibiotics' polyketide backbone	Amycolatopsis mediterranei