Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

ChainsTypeFamily Name Domain Identifier Family IdentifierProvenance Source (Version)
ASCOP2 FamilyPenicillin acylase catalytic domain8025335 4002245 SCOP2 (2022-06-29)
ASCOP2 SuperfamilyClass II glutamine amidotransferases8037714 3000131 SCOP2 (2022-06-29)
BSCOP2B SuperfamilyClass II glutamine amidotransferases8037714 3000131 SCOP2B (2022-06-29)

Domain Annotation: ECOD Classification ECOD Database Homepage

ChainsFamily NameDomain Identifier ArchitecturePossible HomologyHomologyTopologyFamilyProvenance Source (Version)
APenicil_amidasee3s8rA1 A: a+b four layersX: Ntn/PP2CH: NtnT: Penicillin acylase, catalytic domainF: Penicil_amidaseECOD (1.6)
BPenicil_amidasee3s8rB1 A: a+b four layersX: Ntn/PP2CH: NtnT: Penicillin acylase, catalytic domainF: Penicil_amidaseECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Protein Family Annotation Pfam Database Homepage

ChainsAccessionNameDescriptionCommentsSource
A, B
PF01804Penicillin amidase (Penicil_amidase)Penicillin amidase- Family

Structure Motif Annotation: Mechanism and Catalytic Site Atlas M-CSA Database Homepage

ChainsEnzyme NameDescriptionCatalytic Residues
glutaryl-7-aminocephalosporanic-acid acylase  M-CSA #288

Glutaryl 7-aminocephalosporanic acid (7-ACA) acylase catalyses the hydrolysis of Glutaryl 7-ACA to Glutaric acid and 7-ACA. It belongs to the family of N-terminal hydrolase (peptidase S45 family). 7-ACA is the starting compound for the synthesis of cephalosporin antibiotics and it is usually obtained industrially by chemical deacylation of cephalosporin C(CPC). Since the chemical production of 7-ACA is expensive and produce toxic chemical wastes, the enzymatic conversion of CPC to 7-ACA by 7-ACA acylase is of great interest.

In order for the enzyme to be activated towards catalysing the hydrolysis of the glutaryl form of 7-aminocephalosporanic acid, autoproteolysis must occur at the nucleophilic Ser170, revealing an N terminal nucleophile capable of inducing nucleophilic attack at the substrate's glutaryl carbonyl. The process forms two descrete proteins chains. The crystal structure depicts the non-cleaved, precursor protein, whereas the active protein froms a heterotetramer from the two resulting chains.

Defined by 5 residues: ALA:A-170HIS:A-192VAL:A-239ASN:A-413GLU:A-624
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