1FM2
THE 2 ANGSTROM CRYSTAL STRUCTURE OF CEPHALOSPORIN ACYLASE
Summary for 1FM2
Entry DOI | 10.2210/pdb1fm2/pdb |
Descriptor | GLUTARYL 7-AMINOCEPHALOSPORANIC ACID ACYLASE (3 entities in total) |
Functional Keywords | cephalosporin acylase, antibiotics, penicillin acylase, n-terminal hydrolase, hydrolase |
Biological source | Brevundimonas diminuta More |
Cellular location | Periplasm : Q9L5D6 Q9L5D6 |
Total number of polymer chains | 2 |
Total formula weight | 77253.48 |
Authors | Kim, Y.,Yoon, K.H.,Khang, Y.,Turley, S.,Hol, W.G.J. (deposition date: 2000-08-15, release date: 2001-08-15, Last modification date: 2024-11-20) |
Primary citation | Kim, Y.,Yoon, K.,Khang, Y.,Turley, S.,Hol, W.G. The 2.0 A crystal structure of cephalosporin acylase. Structure Fold.Des., 8:1059-1068, 2000 Cited by PubMed Abstract: Semisynthetic cephalosporins are primarily synthesized from 7-aminocephalosporanic acid (7-ACA), which is usually obtained by chemical deacylation of cephalosporin C (CPC). The chemical production of 7-ACA includes, however, several expensive steps and requires thorough treatment of chemical wastes. Therefore, an enzymatic conversion of CPC to 7-ACA by cephalosporin acylase is of great interest. The biggest obstacle preventing this in industrial production is that cephalosporin acylase uses glutaryl-7ACA as a primary substrate and has low substrate specificity for CPC. PubMed: 11080627DOI: 10.1016/S0969-2126(00)00505-0 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2 Å) |
Structure validation
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