title: Metal-characterization of N-acyl-D-glutamate amidohydrolase from Pseudomonas sp. strain 5f-1.
abstract: N-Acyl-D-glutamate amidohydrolase (D-AGase) from Pseudomonas sp. 5f-1 was a zinc-metalloenzyme which contained 2.06-2.61 g.atom of Zn per mole of enzyme. The zinc atom was required for the catalytic activity and stability of the enzyme. The N-terminal amino acid sequence of Pseudomonas sp. 5f-1 D-AGase showed 32% identity to that of Alcaligenes xylosoxydans subsp. xylosoxydans A-6.
authors.affiliation: Department of Applied Chemistry, Faculty of Engineering, Oita University, Japan.
authors.forename: M
authors.initials: M
authors.lastname: Wakayama
authors.forename: Y
authors.initials: Y
authors.lastname: Miura
authors.forename: K
authors.initials: K
authors.lastname: Oshima
authors.forename: K
authors.initials: K
authors.lastname: Sakai
authors.forename: M
authors.initials: M
authors.lastname: Moriguchi
mesh_terms: D000581:Amidohydrolases / Q000037:antagonists & inhibitors / Q000737:chemistry / Q000378:metabolism*; D000595:Amino Acid Sequence; D000596:Amino Acids / Q000032:analysis; D002614:Chelating Agents / Q000494:pharmacology; D004492:Edetic Acid / Q000494:pharmacology; D004789:Enzyme Activation; D004791:Enzyme Inhibitors / Q000494:pharmacology; D004795:Enzyme Stability; D006358:Hot Temperature; D006863:Hydrogen-Ion Concentration; D007477:Ions; D008969:Molecular Sequence Data; D010618:Phenanthrolines / Q000494:pharmacology; D011549:Pseudomonas / Q000201:enzymology*; D017386:Sequence Homology, Amino Acid; D013997:Time Factors; D015032:Zinc / Q000378:metabolism*
chemical_list: D000596:Amino Acids; D002614:Chelating Agents; D004791:Enzyme Inhibitors; D007477:Ions; D010618:Phenanthrolines; D004492:Edetic Acid; D000581:Amidohydrolases; C070988:N-acyl-D-glutamate deacylase; D015032:Zinc; C025205:1,10-phenanthroline