DB code: M00309

RLCP classification 1.13.30010.30 : Hydrolysis
CATH domain 1.10.439.10 : Penicillin Amidohydrolase; domain 1
3.60.20.10 : Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1 Catalytic domain
2.30.120.10 : Penicillin G acylase, beta-roll domain
1.10.1400.10 : Penicillin amidase (Acylase) alpha subunit, N-terminal domain
E.C. 3.5.1.93
CSA
M-CSA
MACiE M0288

CATH domain Related DB codes (homologues)

Uniprot Enzyme Name
UniprotKB Protein name Synonyms Contains MEROPS Pfam
Q9L5D6 Glutaryl-7-aminocephalosporanic-acid acylase
Glutaryl-7-ACA acylase
EC 3.5.1.93
7-beta-(4-carboxybutanamido)cephalosporanic acid acylase
CAD
GL-7-ACA acylase
GCA
Glutaryl-7-aminocephalosporanic-acid acylase subunit alpha
(Glutaryl-7-ACA acylase subunit alpha)
Glutaryl-7-aminocephalosporanic-acid acylase subunit beta
(Glutaryl-7-ACA acylase subunit beta)
S45.002 (Serine)
PF01804 (Penicil_amidase)
[Graphical View]
P07662 Glutaryl-7-aminocephalosporanic-acid acylase
Glutaryl-7-ACA acylase
EC 3.5.1.93
7-beta-(4-carboxybutanamido)cephalosporanic acid acylase
GL-7-ACA acylase
GCA
Glutaryl-7-aminocephalosporanic-acid acylase subunit alpha
(Glutaryl-7-ACA acylase subunit alpha)
Glutaryl-7-aminocephalosporanic-acid acylase subunit beta
(Glutaryl-7-ACA acylase subunit beta)
S45.002 (Serine)
PF01804 (Penicil_amidase)
[Graphical View]
O86089
Cephalosporin acylase
None S45.002 (Serine)
PF01804 (Penicil_amidase)
[Graphical View]

KEGG enzyme name
Glutaryl-7-aminocephalosporanic-acid acylase
7Beta-(4-carboxybutanamido)cephalosporanic acid acylase
Cephalosporin C acylase
Glutaryl-7-ACA acylase
CA
GCA
GA
Cephalosporin acylase
Glutaryl-7-aminocephalosporanic acid acylase
GL-7-ACA acylase

UniprotKB: Accession Number Entry name Activity Subunit Subcellular location Cofactor
Q9L5D6 G7AC_BREDI (7R)-7-(4-carboxybutanamido)cephalosporanate + H(2)O = (7R)-7-aminocephalosporanate + glutarate. Heterodimer of a small subunit and a large subunit processed from the same precursor. Periplasm (Potential).
P07662 G7AC_PSEU7 (7R)-7-(4-carboxybutanamido)cephalosporanate + H2O = (7R)-7-aminocephalosporanate + glutarate. Heterotetramer of two alpha and two beta subunits processed from the same precursor. Periplasm
O86089 O86089_9PROT

KEGG Pathways
Map code Pathways E.C.
MAP00311 Penicillin and cephalosporin biosynthesis

Compound table
Substrates Products Intermediates
KEGG-id C15666 C00001 C07756 C00489 I00190 I00191 I00192
E.C.
Compound (7R)-7-(4-carboxybutanamido)cephalosporanate H2O (7R)-7-aminocephalosporanate glutarate Peptidyl-Ser-7-glutarylaminocephalosporanate (tetrahedral transition-state) Peptidyl-Ser-glutarate (acyl-enzyme intermediate) Peptidyl-Ser-glutarate (tetrahedral transition-state)
Type amide group,carbohydrate,carboxyl group,sulfide group H2O amide group,amine group,carbohydrate,carboxyl group,sulfide group carboxyl group
ChEBI 15377
PubChem 22247451
962
1kehA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound
1fm2A00 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound
1jvzA00 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound
1jw0A00 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound
3s8rA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound
3s8rB02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound
1or0A00 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound
1or0C00 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound
1gk0A00 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound
1gk0C00 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound
1gk1A00 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound
1gk1C00 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound
1ghdA00 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound
2ae3A00 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound
2ae4A00 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound
2ae5A00 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound
1kehA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound
1fm2B01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound
1jvzB01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Bound:CEN Unbound Unbound Unbound Unbound Unbound
1jw0B01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Bound:GUA Unbound Unbound Unbound
3s8rA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound
3s8rB01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound
1or0B01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound
1or0D01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound
1gk0B01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Transition-state-analogue:PO4-EDO
1gk0D01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Transition-state-analogue:PO4-EDO
1gk1B01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound
1gk1D01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound
1ghdB01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound
2ae3B01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound
2ae4B01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound
2ae5B01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound
1kehA03 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound
1fm2B03 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound
1jvzB03 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound
1jw0B03 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound
3s8rA03 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound
3s8rB03 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound
1or0B03 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound
1or0D03 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound
1gk0B03 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound
1gk0D03 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound
1gk1B03 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound
1gk1D03 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound
1ghdB03 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound
2ae3B02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound
2ae4B02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound
2ae5B02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound
1kehA04 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound
1fm2B02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound
1jvzB02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound
1jw0B02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound
3s8rA04 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound
3s8rB04 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound
1or0B02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound
1or0D02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound
1gk0B02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound
1gk0D02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound
1gk1B02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound
1gk1D02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound
1ghdB02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound
2ae3B03 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound
2ae4B03 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound
2ae5B03 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound

Reference for Active-site residues
resource references E.C.

Active-site residues
PDB Catalytic residues Cofactor-binding residues Modified residues Main-chain involved in catalysis Comment
1kehA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
1fm2A00 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
1jvzA00 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
1jw0A00 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
3s8rA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
3s8rB02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
1or0A00 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
1or0C00 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
1gk0A00 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
1gk0C00 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
1gk1A00 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
1gk1C00 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
1ghdA00 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
2ae3A00 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
2ae4A00 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
2ae5A00 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
1kehA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ;HIS 192;ASN 413 ;HIS 192;VAL 239 mutant S170A
1fm2B01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain SER 170;HIS 192;ASN 413 SER 170;HIS 192;VAL 239
1jvzB01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain SER 170;HIS 192;ASN 413 SER 170;HIS 192;VAL 239
1jw0B01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain SER 170;HIS 192;ASN 413 SER 170;HIS 192;VAL 239
3s8rA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ;HIS 192;ASN 413 ;HIS 192;VAL 239 mutant S170A
3s8rB01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ;HIS 192;ASN 413 ;HIS 192;VAL 239 mutant S170A
1or0B01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain SER 1;HIS 23;ASN 244 SER 1;HIS 23;VAL 70
1or0D01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain SER 1;HIS 23;ASN 244 SER 1;HIS 23;VAL 70
1gk0B01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain SER 1;HIS 23;ASN 244 SER 1;HIS 23;VAL 70
1gk0D01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain SER 1;HIS 23;ASN 244 SER 1;HIS 23;VAL 70
1gk1B01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain SER 1;HIS 23;ASN 244 SER 1;HIS 23;VAL 70
1gk1D01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain SER 1;HIS 23;ASN 244 SER 1;HIS 23;VAL 70
1ghdB01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain SER 1;HIS 23;ASN 244 SER 1;HIS 23;VAL 70
2ae3B01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain SER 1;HIS 23;ASN 244 SER 1;HIS 23;VAL 70
2ae4B01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain SER 1;HIS 23;ASN 244 SER 1;HIS 23;VAL 70
2ae5B01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ;HIS 23;ASN 244 SER 1;HIS 23;VAL 70 mutant S1C
1kehA03 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
1fm2B03 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
1jvzB03 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
1jw0B03 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
3s8rA03 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
3s8rB03 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
1or0B03 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
1or0D03 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
1gk0B03 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
1gk0D03 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
1gk1B03 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
1gk1D03 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
1ghdB03 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
2ae3B02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
2ae4B02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
2ae5B02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
1kehA04 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
1fm2B02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
1jvzB02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
1jw0B02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
3s8rA04 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
3s8rB04 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
1or0B02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
1or0D02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
1gk0B02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
1gk0D02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
1gk1B02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
1gk1D02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
1ghdB02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
2ae3B03 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
2ae4B03 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
2ae5B03 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain

References for Catalytic Mechanism
References Sections No. of steps in catalysis
[4]
p.1063
[10]
p.95-97

References
[1]
Resource
Comments
Medline ID
PubMed ID 11099866
Journal Biochim Biophys Acta
Year 2000
Volume 1523
Pages 123-7
Authors Lee YS, Kim HW, Lee KB, Park SS
Title Involvement of arginine and tryptophan residues in catalytic activity of glutaryl 7-aminocephalosporanic acid acylase from Pseudomonas sp. strain GK16.
Related PDB
Related UniProtKB
[2]
Resource
Comments
Medline ID
PubMed ID 10991936
Journal J Biol Chem
Year 2000
Volume 275
Pages 39200-6
Authors Lee YS, Kim HW, Park SS
Title The role of alpha-amino group of the N-terminal serine of beta subunit for enzyme catalysis and autoproteolytic activation of glutaryl 7-aminocephalosporanic acid acylase.
Related PDB
Related UniProtKB
[3]
Resource
Comments
Medline ID
PubMed ID 10945972
Journal J Struct Biol
Year 2000
Volume 131
Pages 79-81
Authors Kwon TH, Rhee S, Lee YS, Park SS, Kim KH
Title Crystallization and preliminary X-Ray diffraction analysis of glutaryl-7-aminocephalosporanic acid acylase from Pseudomonas sp. GK16.
Related PDB
Related UniProtKB
[4]
Resource
Comments
Medline ID
PubMed ID 11080627
Journal Structure
Year 2000
Volume 8
Pages 1059-68
Authors Kim Y, Yoon K, Khang Y, Turley S, Hol WG
Title The 2.0 A crystal structure of cephalosporin acylase.
Related PDB 1fm2
Related UniProtKB
[5]
Resource
Comments
Medline ID
PubMed ID 11755403
Journal Chem Biol
Year 2001
Volume 8
Pages 1253-64
Authors Kim Y, Hol WG
Title Structure of cephalosporin acylase in complex with glutaryl-7-aminocephalosporanic acid and glutarate: insight into the basis of its substrate specificity.
Related PDB 1jvz 1jw0
Related UniProtKB
[6]
Resource
Comments
Medline ID
PubMed ID 11604409
Journal J Biol Chem
Year 2001
Volume 276
Pages 48376-81
Authors Kim S, Kim Y
Title Active site residues of cephalosporin acylase are critical not only for enzymatic catalysis but also for post-translational modification.
Related PDB
Related UniProtKB
[7]
Resource
Comments
Medline ID
PubMed ID 11782466
Journal J Biol Chem
Year 2002
Volume 277
Pages 10256-64
Authors Huang X, Zeng R, Ding X, Mao X, Ding Y, Rao Z, Xie Y, Jiang W, Zhao G
Title Affinity alkylation of the Trp-B4 residue of the beta -subunit of the glutaryl 7-aminocephalosporanic acid acylase of Pseudomonas sp. 130.
Related PDB
Related UniProtKB
[8]
Resource
Comments
Medline ID
PubMed ID 11706000
Journal J Biol Chem
Year 2002
Volume 277
Pages 2823-9
Authors Kim Y, Kim S, Earnest TN, Hol WG
Title Precursor structure of cephalosporin acylase. Insights into autoproteolytic activation in a new N-terminal hydrolase family.
Related PDB 1keh
Related UniProtKB
[9]
Resource
Comments
Medline ID
PubMed ID 12198140
Journal J Biol Chem
Year 2002
Volume 277
Pages 42121-7
Authors Otten LG, Sio CF, Vrielink J, Cool RH, Quax WJ
Title Altering the substrate specificity of cephalosporin acylase by directed evolution of the Beta -subunit.
Related PDB
Related UniProtKB
[10]
Resource
Comments
Medline ID
PubMed ID 11742126
Journal Protein Sci
Year 2002
Volume 11
Pages 92-103
Authors Fritz-Wolf K, Koller KP, Lange G, Liesum A, Sauber K, Schreuder H, Aretz W, Kabsch W
Title Structure-based prediction of modifications in glutarylamidase to allow single-step enzymatic production of 7-aminocephalosporanic acid from cephalosporin C.
Related PDB 1gk1 1gk0
Related UniProtKB
[11]
Resource
Comments
Medline ID
PubMed ID 14511642
Journal Biochem Biophys Res Commun
Year 2003
Volume 310
Pages 19-27
Authors Oh B, Kim M, Yoon J, Chung K, Shin Y, Lee D, Kim Y
Title Deacylation activity of cephalosporin acylase to cephalosporin C is improved by changing the side-chain conformations of active-site residues.
Related PDB
Related UniProtKB
[12]
Resource
Comments
Medline ID
PubMed ID 14680829
Journal Biochem Biophys Res Commun
Year 2003
Volume 312
Pages 755-60
Authors Sio CF, Otten LG, Cool RH, Quax WJ
Title Analysis of a substrate specificity switch residue of cephalosporin acylase.
Related PDB
Related UniProtKB
[13]
Resource
Comments
Medline ID
PubMed ID 12680762
Journal Biochemistry
Year 2003
Volume 42
Pages 4084-93
Authors Kim JK, Yang IS, Rhee S, Dauter Z, Lee YS, Park SS, Kim KH
Title Crystal structures of glutaryl 7-aminocephalosporanic acid acylase: insight into autoproteolytic activation.
Related PDB 3s8r 1or0
Related UniProtKB
[14]
Resource
Comments
Medline ID
PubMed ID 15174165
Journal Chembiochem
Year 2004
Volume 5
Pages 820-5
Authors Otten LG, Sio CF, van der Sloot AM, Cool RH, Quax WJ
Title Mutational analysis of a key residue in the substrate specificity of a cephalosporin acylase.
Related PDB
Related UniProtKB
[15]
Resource
Comments
Medline ID
PubMed ID 15200051
Journal Protein J
Year 2004
Volume 23
Pages 197-204
Authors Mao X, Wang W, Jiang W, Zhao GP
Title His23beta and Glu455beta of the Pseudomonas sp. 130 glutaryl-7-amino cephalosporanic acid acylase are crucially important for efficient autoproteolysis and enzymatic catalysis.
Related PDB
Related UniProtKB
[16]
Resource
Comments
Medline ID
PubMed ID 16446446
Journal Proc Natl Acad Sci U S A
Year 2006
Volume 103
Pages 1732-7
Authors Kim JK, Yang IS, Shin HJ, Cho KJ, Ryu EK, Kim SH, Park SS, Kim KH
Title Insight into autoproteolytic activation from the structure of cephalosporin acylase: a protein with two proteolytic chemistries.
Related PDB 2adv 2ae3 2ae4 2ae5
Related UniProtKB
[17]
Resource
Comments
Medline ID
PubMed ID 19800869
Journal Biochem Biophys Res Commun
Year 2009
Volume 390
Pages 342-8
Authors Cho KJ, Kim JK, Lee JH, Shin HJ, Park SS, Kim KH
Title Structural features of cephalosporin acylase reveal the basis of autocatalytic activation.
Related PDB
Related UniProtKB
[18]
Resource
Comments
Medline ID
PubMed ID 20606279
Journal Acta Crystallogr Sect F Struct Biol Cryst Commun
Year 2010
Volume 66
Pages 808-10
Authors Anandan A, Vallet C, Coyle T, Moustafa IM, Vrielink A
Title Crystallization and preliminary diffraction analysis of an engineered cephalosporin acylase.
Related PDB
Related UniProtKB
[19]
Resource
Comments
Medline ID
PubMed ID 21576250
Journal J Biol Chem
Year 2011
Volume 286
Pages 24476-86
Authors Yin J, Deng Z, Zhao G, Huang X
Title The N-terminal nucleophile serine of cephalosporin acylase executes the second autoproteolytic cleavage and acylpeptide hydrolysis.
Related PDB
Related UniProtKB

Comments
This enzyme belongs to the Ntn hydrolase family (CATH 3.60.20.10), whose N-terminal residue plays a catalytic residue (see [2]). Moreover, this enzyme belongs to S45 peptidase family (see [19]).
The precursor protein of this enzyme is composed of signal peptide, alpha-subunit, beta-subunit and spaceer-sequence, which is between alpha-subunit and beta-subunit regions ([4], [8], [10], [13], [14], [15], [16], [19]). This precursor protein is activated by a two-step autoproteolysis ([2], [8], [13], [14], [15], [16], [19]).
The first step of the autoproteolytic activation is an intramolecular cleavage of the precursor protein between Gly169 and Ser170 to release alpha'-subunit, which contains spacer sequence, and beta-subunit ([8], [13], [14], [15], [16], [19]). At this step, Ser170 play a nucleophilic role, to attack on the carbonyl carbon of Gly169 (see [8], [13], [16], [19]). This nucleophilic attack leads to formation of tetrahedral transition-state that is stabilized by Asn413 and an oxyanion hole of His192 and Val239 ([13]).
The second step is a cleavage of the alpha'-subunit between Gly160 and Asp161, to produce alpha-subunit and the spacer peptide ([8], [13], [14], [15], [16], [19]). Initially, the second cleavage is thought to proceed by intermolecular interaction (see [2], [6], [8], [12]). More recently, it is reported that the second cleavage step is an intramolecular reaction, in which Ser170 (or Ser1 of beta subunit) plays a nucleophicil role ([16], [19]).
The catalytic reaction of this enzyme may proceed as follows ([4], [10]):
(0) The sidechain of His23-beta (His192 of 1fm2B) maintains the uncharged state of the alpha-amino group of Ser1-beta (Ser170). Here, Glu455-beta may modulate the activity of His23-beta. His23-beta and Glu455-beta form a catalytic dyad ([10]).
(1) The alpha-amino group of Ser1-beta (Ser170) acts as a general base, to activate the sidechain hydroxyl group of Ser1-beta through a water molecule.
(2) Ser1-beta makes a nucleophilic attack on the acyl group of the substrate, leading to a tetrahedral transition-state (I00190).
(3) The negatively charged transition-state is stabilized by an oxyanion hole formed by two amide groups; Mainchain amide groups of His23-beta (His192) and Val70-beta (Val239) and sidechain amide of Asn244-beta (Asn413).
(4) (The amino group of Ser1-beta may act as a general acid to protonate the tetrahedral transition-state, which will lead to collapse of the tetrahedral transition-state.) The collapse of the tetrahedral transition-state leads to a seryl acyl-enzyme intermediate (I00191), releasing 7-aminochephalosporanate (C07756).
(5) Another water molecule, which may be activated by the amino group of Ser1-beta, attacks on the acyl-enzyme intermediate (I00191), leading to another tetrahedral transition-state (I00192). This transition-state (I00192) is also stabilized by the oxyanion hole.
(6) Finally, this transition-state collapses, releasing free glutarate.

Created Updated
2013-02-25 2016-01-27