UniProt functional annotation for P26918



	UniProt functional annotation for P26918

UniProt code: P26918.

Organism: Aeromonas hydrophila.

Taxonomy: Bacteria; Proteobacteria; Gammaproteobacteria; Aeromonadales; Aeromonadaceae; Aeromonas.

Function: Confers resistance to the different beta-lactams antibiotics (penicillin, cephalosporin and carbapenem) via the hydrolysis of the beta-lactam ring (PubMed:15588826, PubMed:17307979, PubMed:1856163, PubMed:19651913, PubMed:2327760). It is able to hydrolyze penicillin and imipenem, but is much less active against cephalothin, cefotaxime, meropenem and ceftazidime (PubMed:1856163, PubMed:2327760). {ECO:0000269|PubMed:15588826, ECO:0000269|PubMed:17307979, ECO:0000269|PubMed:1856163, ECO:0000269|PubMed:19651913, ECO:0000269|PubMed:2327760}.

Catalytic activity: Reaction=a beta-lactam + H2O = a substituted beta-amino acid; Xref=Rhea:RHEA:20401, ChEBI:CHEBI:15377, ChEBI:CHEBI:35627, ChEBI:CHEBI:140347; EC=3.5.2.6; Evidence={ECO:0000269|PubMed:15588826, ECO:0000269|PubMed:17307979, ECO:0000269|PubMed:19651913, ECO:0000269|PubMed:2327760};

Cofactor: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000269|PubMed:15588826, ECO:0000269|PubMed:17307979, ECO:0000269|PubMed:18563261, ECO:0000269|PubMed:19651913, ECO:0000269|PubMed:20527888}; Note=Binds 1 Zn(2+) ions per subunit. {ECO:0000269|PubMed:15588826, ECO:0000269|PubMed:17307979, ECO:0000269|PubMed:18563261, ECO:0000269|PubMed:19651913, ECO:0000269|PubMed:20527888};

Activity regulation: Competitively inhibited by mercaptophosphonate and pyridine carboxylate derivatives (PubMed:17307979, PubMed:20527888). Also inhibited by the binding of a second zinc ion and by chelating agents such as EDTA (PubMed:1856163, PubMed:2327760, PubMed:19651913). {ECO:0000269|PubMed:17307979, ECO:0000269|PubMed:1856163, ECO:0000269|PubMed:19651913, ECO:0000269|PubMed:20527888, ECO:0000269|PubMed:2327760}.

Biophysicochemical properties: Kinetic parameters: KM=0.8 uM for cefuroxime {ECO:0000269|PubMed:2327760}; KM=9 uM for ceftazidime {ECO:0000269|PubMed:2327760}; KM=15 uM for cefotaxime {ECO:0000269|PubMed:2327760}; KM=19 uM for cloxacillin {ECO:0000269|PubMed:2327760}; KM=28 uM for cephalothin {ECO:0000269|PubMed:2327760}; KM=30 uM for imipenem {ECO:0000269|PubMed:2327760}; KM=30.6 uM for nitrocefin {ECO:0000269|PubMed:2327760}; KM=53.3 uM for aztreonam {ECO:0000269|PubMed:2327760}; KM=63 uM for imipenem (at pH 9) {ECO:0000269|PubMed:17307979}; KM=83 uM for imipenem (at pH 8) {ECO:0000269|PubMed:17307979}; KM=120 uM for imipenem (at pH 7) {ECO:0000269|PubMed:17307979}; KM=124 uM for penicillin G {ECO:0000269|PubMed:2327760}; KM=166 uM for biapenem {ECO:0000269|PubMed:15588826}; KM=340 uM for imipenem {ECO:0000269|PubMed:15588826, ECO:0000269|PubMed:19651913}; KM=1300 uM for nitrocefin {ECO:0000269|PubMed:15588826, ECO:0000269|PubMed:19651913}; Vmax=170 umol/min/mg enzyme with penicillin G as substrate {ECO:0000269|PubMed:2327760}; Vmax=100 umol/min/mg enzyme with nitrocefin as substrate {ECO:0000269|PubMed:2327760}; Vmax=68.5 umol/min/mg enzyme with imipenem as substrate {ECO:0000269|PubMed:2327760}; Vmax=12.8 umol/min/mg enzyme with cefuroxime as substrate {ECO:0000269|PubMed:2327760}; Vmax=3.2 umol/min/mg enzyme with aztreonam as substrate {ECO:0000269|PubMed:2327760}; Vmax=1.8 umol/min/mg enzyme with cephalothin as substrate {ECO:0000269|PubMed:2327760}; Vmax=1.1 umol/min/mg enzyme with cloxacillin as substrate {ECO:0000269|PubMed:2327760}; Vmax=0.5 umol/min/mg enzyme with cefotaxime as substrate {ECO:0000269|PubMed:2327760}; Vmax=0.3 umol/min/mg enzyme with ceftazidime as substrate {ECO:0000269|PubMed:2327760}; Note=Kcat is 1200 sec(-1) for lactamase activity with imipenem as substrate (PubMed:15588826, PubMed:19651913). Kcat is 300 sec(-1) for lactamase activity with biapenem as substrate (PubMed:15588826). Kcat is 210 sec(-1) for lactamase activity with imipenem as substrate (at pH 7) (PubMed:17307979). Kcat is 140 sec(-1) for lactamase activity with imipenem as substrate (at pH 8) (PubMed:17307979). Kcat is 49 sec(-1) for lactamase activity with imipenem as substrate (at pH 9) (PubMed:17307979). Kcat is 0.008 sec(-1) for lactamase activity with nitrocefin as substrate (PubMed:19651913). {ECO:0000269|PubMed:15588826, ECO:0000269|PubMed:17307979, ECO:0000269|PubMed:19651913};

Subunit: Monomer. {ECO:0000269|PubMed:15588826, ECO:0000269|PubMed:1856163, ECO:0000269|PubMed:2327760}.

Subcellular location: Periplasm {ECO:0000305|PubMed:1856163}.

Induction: By either cefoxitin or imipenem. {ECO:0000269|PubMed:2327760}.

Similarity: Belongs to the metallo-beta-lactamase superfamily. Class-B beta-lactamase family. {ECO:0000305}.

Annotations taken from UniProtKB at the EBI.


Organism:		Aeromonas hydrophila.
Taxonomy:		Bacteria; Proteobacteria; Gammaproteobacteria; Aeromonadales; Aeromonadaceae; Aeromonas.



Function:		Confers resistance to the different beta-lactams antibiotics (penicillin, cephalosporin and carbapenem) via the hydrolysis of the beta-lactam ring (PubMed:15588826, PubMed:17307979, PubMed:1856163, PubMed:19651913, PubMed:2327760). It is able to hydrolyze penicillin and imipenem, but is much less active against cephalothin, cefotaxime, meropenem and ceftazidime (PubMed:1856163, PubMed:2327760). {ECO:0000269\|PubMed:15588826, ECO:0000269\|PubMed:17307979, ECO:0000269\|PubMed:1856163, ECO:0000269\|PubMed:19651913, ECO:0000269\|PubMed:2327760}.


Catalytic activity:		Reaction=a beta-lactam + H2O = a substituted beta-amino acid; Xref=Rhea:RHEA:20401, ChEBI:CHEBI:15377, ChEBI:CHEBI:35627, ChEBI:CHEBI:140347; EC=3.5.2.6; Evidence={ECO:0000269\|PubMed:15588826, ECO:0000269\|PubMed:17307979, ECO:0000269\|PubMed:19651913, ECO:0000269\|PubMed:2327760};
Cofactor:		Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000269\|PubMed:15588826, ECO:0000269\|PubMed:17307979, ECO:0000269\|PubMed:18563261, ECO:0000269\|PubMed:19651913, ECO:0000269\|PubMed:20527888}; Note=Binds 1 Zn(2+) ions per subunit. {ECO:0000269\|PubMed:15588826, ECO:0000269\|PubMed:17307979, ECO:0000269\|PubMed:18563261, ECO:0000269\|PubMed:19651913, ECO:0000269\|PubMed:20527888};
Activity regulation:		Competitively inhibited by mercaptophosphonate and pyridine carboxylate derivatives (PubMed:17307979, PubMed:20527888). Also inhibited by the binding of a second zinc ion and by chelating agents such as EDTA (PubMed:1856163, PubMed:2327760, PubMed:19651913). {ECO:0000269\|PubMed:17307979, ECO:0000269\|PubMed:1856163, ECO:0000269\|PubMed:19651913, ECO:0000269\|PubMed:20527888, ECO:0000269\|PubMed:2327760}.
Biophysicochemical properties:		Kinetic parameters: KM=0.8 uM for cefuroxime {ECO:0000269\|PubMed:2327760}; KM=9 uM for ceftazidime {ECO:0000269\|PubMed:2327760}; KM=15 uM for cefotaxime {ECO:0000269\|PubMed:2327760}; KM=19 uM for cloxacillin {ECO:0000269\|PubMed:2327760}; KM=28 uM for cephalothin {ECO:0000269\|PubMed:2327760}; KM=30 uM for imipenem {ECO:0000269\|PubMed:2327760}; KM=30.6 uM for nitrocefin {ECO:0000269\|PubMed:2327760}; KM=53.3 uM for aztreonam {ECO:0000269\|PubMed:2327760}; KM=63 uM for imipenem (at pH 9) {ECO:0000269\|PubMed:17307979}; KM=83 uM for imipenem (at pH 8) {ECO:0000269\|PubMed:17307979}; KM=120 uM for imipenem (at pH 7) {ECO:0000269\|PubMed:17307979}; KM=124 uM for penicillin G {ECO:0000269\|PubMed:2327760}; KM=166 uM for biapenem {ECO:0000269\|PubMed:15588826}; KM=340 uM for imipenem {ECO:0000269\|PubMed:15588826, ECO:0000269\|PubMed:19651913}; KM=1300 uM for nitrocefin {ECO:0000269\|PubMed:15588826, ECO:0000269\|PubMed:19651913}; Vmax=170 umol/min/mg enzyme with penicillin G as substrate {ECO:0000269\|PubMed:2327760}; Vmax=100 umol/min/mg enzyme with nitrocefin as substrate {ECO:0000269\|PubMed:2327760}; Vmax=68.5 umol/min/mg enzyme with imipenem as substrate {ECO:0000269\|PubMed:2327760}; Vmax=12.8 umol/min/mg enzyme with cefuroxime as substrate {ECO:0000269\|PubMed:2327760}; Vmax=3.2 umol/min/mg enzyme with aztreonam as substrate {ECO:0000269\|PubMed:2327760}; Vmax=1.8 umol/min/mg enzyme with cephalothin as substrate {ECO:0000269\|PubMed:2327760}; Vmax=1.1 umol/min/mg enzyme with cloxacillin as substrate {ECO:0000269\|PubMed:2327760}; Vmax=0.5 umol/min/mg enzyme with cefotaxime as substrate {ECO:0000269\|PubMed:2327760}; Vmax=0.3 umol/min/mg enzyme with ceftazidime as substrate {ECO:0000269\|PubMed:2327760}; Note=Kcat is 1200 sec(-1) for lactamase activity with imipenem as substrate (PubMed:15588826, PubMed:19651913). Kcat is 300 sec(-1) for lactamase activity with biapenem as substrate (PubMed:15588826). Kcat is 210 sec(-1) for lactamase activity with imipenem as substrate (at pH 7) (PubMed:17307979). Kcat is 140 sec(-1) for lactamase activity with imipenem as substrate (at pH 8) (PubMed:17307979). Kcat is 49 sec(-1) for lactamase activity with imipenem as substrate (at pH 9) (PubMed:17307979). Kcat is 0.008 sec(-1) for lactamase activity with nitrocefin as substrate (PubMed:19651913). {ECO:0000269\|PubMed:15588826, ECO:0000269\|PubMed:17307979, ECO:0000269\|PubMed:19651913};
Subunit:		Monomer. {ECO:0000269\|PubMed:15588826, ECO:0000269\|PubMed:1856163, ECO:0000269\|PubMed:2327760}.
Subcellular location:		Periplasm {ECO:0000305\|PubMed:1856163}.
Induction:		By either cefoxitin or imipenem. {ECO:0000269\|PubMed:2327760}.
Similarity:		Belongs to the metallo-beta-lactamase superfamily. Class-B beta-lactamase family. {ECO:0000305}.