Cephalosporin acylase

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Revision as of 10:16, 11 February 2019

Cephalosporin acylase α subunit (magenta) and β subunit (green) complex with glutarate (PDB entry 1jw0)

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Updated on 11-February-2019

↑ Kim Y, Yoon K, Khang Y, Turley S, Hol WG. The 2.0 A crystal structure of cephalosporin acylase. Structure. 2000 Oct 15;8(10):1059-68. PMID:11080627
↑ Kim Y, Hol WG. Structure of cephalosporin acylase in complex with glutaryl-7-aminocephalosporanic acid and glutarate: insight into the basis of its substrate specificity. Chem Biol. 2001 Dec;8(12):1253-64. PMID:11755403

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 == Structural highlights ==
-<scene name='52/525143/Cv/2'>CSA contains 2 non-identical subunits</scene>.  The <scene name='52/525143/Cv/3'>active site pocket</scene> (PDB entry [[1jw0]])<ref>PMID:11755403</ref> of CSA is similar to that of penicillin acylase.  CSA precursor is cleaved at 2 sites forming the active heterodimer.
+<scene name='52/525143/Cv/2'>CSA contains 2 non-identical subunits</scene>.  The <scene name='52/525143/Cv/4'>active site pocket</scene> (PDB entry [[1jw0]])<ref>PMID:11755403</ref> of CSA is similar to that of penicillin acylase. Water molecules are shoen as red spheres. CSA precursor is cleaved at 2 sites forming the active heterodimer.
 </StructureSection>