Cephalosporin acylase

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
{{STRUCTURE_1jvz| PDB=1jvz | SIZE=400| SCENE= |right|CAPTION=Cephalosporin acylase complex with glutaryl 7-amino-cephalosporanic acid, [[1jvz]] }}
+
{{STRUCTURE_1jvz| PDB=1jvz | SIZE=400| SCENE= |right|CAPTION=Cephalosporin acylase α subunit (grey) and β subunit (green) complex with glutaryl 7-amino-cephalosporanic acid, [[1jvz]] }}
'''Cephalosporin acylase''' (CSA) catalyzes the conversion of cephalosporin C (CPC) to 7-amino-cephalosporanic acid (7-ACA). CSA contains 2 non-identical subunits. CSA is used commercially for production of semi-synthetic cephalosporin antibiotics. The active site pocket of CSA is similar to that of penicillin acylase. CSA precursor is cleaved at 2 sites forming the active heterodimer.
'''Cephalosporin acylase''' (CSA) catalyzes the conversion of cephalosporin C (CPC) to 7-amino-cephalosporanic acid (7-ACA). CSA contains 2 non-identical subunits. CSA is used commercially for production of semi-synthetic cephalosporin antibiotics. The active site pocket of CSA is similar to that of penicillin acylase. CSA precursor is cleaved at 2 sites forming the active heterodimer.

Revision as of 11:02, 26 December 2012

Template:STRUCTURE 1jvz

Cephalosporin acylase (CSA) catalyzes the conversion of cephalosporin C (CPC) to 7-amino-cephalosporanic acid (7-ACA). CSA contains 2 non-identical subunits. CSA is used commercially for production of semi-synthetic cephalosporin antibiotics. The active site pocket of CSA is similar to that of penicillin acylase. CSA precursor is cleaved at 2 sites forming the active heterodimer.

3D structures of cephalosporin acylase

2nlz - CSA – Bacillus halodurans
1fm2 - BdCSA – Brevundimonas diminuta
1gk0, 1gk1, 1ghd - PsCSA – Pseudomonas
2ae3, 2ae5 - PsCSA α + β (mutant) subunits
2ae4 - PsCSA α (mutant) + β subunits
1keh - BdCSA precursor (mutant)

Cephalosporin acylase complex

1jvz – BdCSA + glutaryl-7-ACA
1jw0 - BdCSA + glutarate

Proteopedia Page Contributors and Editors (what is this?)

Michal Harel, Alexander Berchansky

Personal tools