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4.2.1.144: 3-amino-5-hydroxybenzoate synthase

This is an abbreviated version!
For detailed information about 3-amino-5-hydroxybenzoate synthase, go to the full flat file.

Word Map on EC 4.2.1.144

Reaction

5-amino-5-deoxy-3-dehydroshikimate
=
3-amino-5-hydroxybenzoate
 +
H2O

Synonyms

3-amino-5-hydroxybenzoic acid synthase, AHBA synthase, rifK

ECTree

     4 Lyases
         4.2 Carbon-oxygen lyases
             4.2.1 Hydro-lyases
                4.2.1.144 3-amino-5-hydroxybenzoate synthase

Crystallization

Crystallization on EC 4.2.1.144 - 3-amino-5-hydroxybenzoate synthase

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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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