Any feedback?
Please rate this page
(enzyme.php)
(0/150)

BRENDA support

BRENDA Home
show all | hide all No of entries

Information on EC 3.5.2.6 - beta-lactamase and Organism(s) Escherichia coli and UniProt Accession Q840M4

for references in articles please use BRENDA:EC3.5.2.6
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
     3 Hydrolases
         3.5 Acting on carbon-nitrogen bonds, other than peptide bonds
             3.5.2 In cyclic amides
                3.5.2.6 beta-lactamase
IUBMB Comments
A group of enzymes of varying specificity hydrolysing beta-lactams; some act more rapidly on penicillins, some more rapidly on cephalosporins. The latter were formerly listed as EC 3.5.2.8, cephalosporinase.
Specify your search results
Select one or more organisms in this record: ?
This record set is specific for:
Escherichia coli
UNIPROT: Q840M4
Show additional data
Do not include text mining results
Include (text mining) results
Include results (AMENDA + additional results, but less precise)
Word Map
hide
The taxonomic range for the selected organisms is: Escherichia coli
The enzyme appears in selected viruses and cellular organisms
Synonyms
beta-lactamase, carbapenemase, extended-spectrum beta-lactamase, ndm-1, penicillinase, tem-1, blandm-1, ges-1, blactx-m-15, kpc-2, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
extended-spectrum beta-lactamase
-
AmpC beta-lactamase
Beta lactamase OXA-10
-
-
-
-
beta-lactamase
beta-lactamase ACT-1
-
-
beta-lactamase AME I
-
-
-
-
beta-lactamase CMY-1
-
-
beta-lactamase CMY-2
-
-
beta-lactamase II
-
-
-
-
beta-lactamase MIR-1
-
-
beta-lactamase OXA-1
-
-
beta-lactamase OXA-10
-
-
beta-lactamases CTX-M-25
-
beta-lactamse A-D
-
-
BLAIMP
-
-
-
-
blaTEM-1
carbapenemase
-
-
-
-
Carbenicillinase
-
-
-
-
cefotaximase
-
-
-
-
ceftazidimase
-
-
-
-
cefurooximase
-
-
-
-
Cefuroximase
-
-
-
-
Cephalosporinase
cephamycinase
-
-
class A beta-lactamase
-
class A TEM-2 beta-lactamase
-
-
class A TEM-2 enzyme
-
class C cephalosporinase
-
-
class D beta-lactamase
-
class D OXA-1 beta-lactamase
-
CMY-2-type beta-lactamase
-
CTX-M beta-lactamase
-
CTX-M-14
-
-
extended-spectrum beta-lactamase
Imipenem-cefoxitin hydrolyzing enzyme
-
-
-
-
imipenemase
-
-
-
-
mbetal L1
-
-
metallo-beta-lactamase
-
-
-
-
metallo-beta-lactamase L1
-
-
MIR-4 beta-lactamase
-
neutrapen
-
-
-
-
New Delhi metallo-beta-lactamase
-
OXA-1
oxa-1 beta-lactamase
OXA-10 enzyme
-
-
Oxacillinase
penicillinase
-
-
-
-
serine beta-lactamase
-
SHV-2A
-
-
-
-
TEM-1
TEM-1 beta-lactamase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
a beta-lactam + H2O = a substituted beta-amino acid
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
carboxylic acid amide hydrolysis
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
beta-lactam hydrolase
A group of enzymes of varying specificity hydrolysing beta-lactams; some act more rapidly on penicillins, some more rapidly on cephalosporins. The latter were formerly listed as EC 3.5.2.8, cephalosporinase.
CAS REGISTRY NUMBER
COMMENTARY hide
9073-60-3
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(6R,7R)-3-[(acetyloxy)methyl]-7-(formylamino)-8-oxo-5-thia-1-azabicyclo[4.2.0]oct-2-ene-2-carboxylate + H2O
(2R)-5-[(acetyloxy)methyl]-2-[(R)-carboxy(formylamino)methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylate
show the reaction diagram
-
-
-
-
?
(6R,7R)-3-[(acetyloxy)methyl]-7-[hydroxy(phenylacetyl)amino]-8-oxo-5-thia-1-azabicyclo[4.2.0]oct-2-ene-2-carboxylate + H2O
(2R)-5-[(acetyloxy)methyl]-2-[(R)-carboxy[hydroxy(phenylacetyl)amino]methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylate
show the reaction diagram
-
-
-
-
?
(6R,7R)-3-[(acetyloxy)methyl]-8-oxo-7-[(thiophen-2-ylacetyl)amino]-5-thia-1-azabicyclo[4.2.0]oct-2-ene-2-carboxylate + H2O
(2R)-5-[(acetyloxy)methyl]-2-[(R)-carboxy[(thiophen-2-ylacetyl)amino]methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylate
show the reaction diagram
-
-
-
-
?
(6R,7S)-3-[(3-carboxy-4-nitro-phenyl)sulfanylmethyl]-8-oxo-7-[(2-thiophen-2-ylacetyl)amino]-5-thia-1-azabicyclo-[4.2.0]-oct-2-ene-2-carboxylic acid + H2O
?
show the reaction diagram
-
-
-
?
6-aminopenicillanic acid + H2O
(2R,4S)-2-[amino(carboxy)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
show the reaction diagram
-
-
-
-
?
7-(thienyl-2-acetamido)-3-[2-(4-N,N-dimethylaminophenylazo)pyridinium-methyl]-3-cephem-4-carboxylic acid + H2O
(2R)-2-[(R)-carboxy{(E)-[1-hydroxy-2-(thiophen-2-yl)ethylidene]amino}methyl]-5-{[(2E)-2-{[4-(dimethyliminio)cyclohexa-2,5-dien-1-ylidene]hydrazinylidene}pyridin-1(2H)-yl]methyl}-3,6-dihydro-2H-1,3-thiazine-4-carboxylate
show the reaction diagram
-
-
-
-
?
7beta-[(thien-2-yl)acetamido]-3-[(4-nitro-3-carboxyphenylthio)methyl]-3-cephem-4-carboxylic acid + H2O
(2R)-2-[(R)-carboxy{(E)-[1-hydroxy-2-(thiophen-2-yl)ethylidene]amino}methyl]-5-{[(3-carboxy-4-nitrophenyl)sulfanyl]methyl}-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
show the reaction diagram
-
-
-
-
?
a penicillin + H2O
a penicilloic acid
show the reaction diagram
-
-
-
?
amikacin + H2O
?
show the reaction diagram
-
-
-
-
?
amoxicillin + H2O
(2R,4S)-2-[(R)-[[(2R)-2-amino-2-(4-hydroxyphenyl)acetyl]amino](carboxy)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
show the reaction diagram
-
-
-
-
?
ampicillin + H2O
(2R,4S)-2-[(R)-[[(2R)-2-amino-2-phenylacetyl]amino](carboxy)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
show the reaction diagram
aztreonam + H2O
[(1S,2S)-1-[[(2Z)-2-(2-ammonio-1,3-thiazol-4-yl)-2-[[(2-carboxypropan-2-yl)oxy]imino]acetyl]amino]-1-carboxypropan-2-yl]sulfamate
show the reaction diagram
benzylpenicillin + H2O
(2R,4S)-2-[(R)-carboxy(2-phenylacetamido)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
show the reaction diagram
carbapenem + H2O
[(2R)-2,3-dihydro-1H-pyrrol-2-yl]acetic acid
show the reaction diagram
-
-
-
-
?
carbenicillin + H2O
(2R,4S)-2-{(R)-carboxy[2-carboxy(phenyl)acetamido]methyl}-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
show the reaction diagram
-
-
-
-
?
cefaclor + H2O
(2R)-2-[(R)-{[(2R)-2-amino-2-phenylacetyl]amino}(carboxy)methyl]-5-chloro-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
show the reaction diagram
-
-
-
-
?
cefaloridine + H2O
(2R)-2-{(R)-carboxy[2-(thiophen-2-yl)acetamido]methyl}-5-[(pyridin-1-ium-1-yl)methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylate
show the reaction diagram
-
-
-
-
?
cefalotin + H2O
(2R)-5-[(acetyloxy)methyl]-2-[(R)-carboxy[2-(thiophen-2-yl)acetamido]methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
show the reaction diagram
-
-
-
?
cefalotin + H2O
(2R)-5-[(acetyloxy)methyl]-2-{(R)-carboxy[2-(thiophen-2-yl)acetamido]methyl}-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
show the reaction diagram
cefamandole + H2O
(2R)-2-[(R)-carboxy{[(2R)-2-hydroxy-2-phenylacetyl]amino}methyl]-5-{[(1-methyl-1H-tetrazol-5-yl)sulfanyl]methyl}-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
show the reaction diagram
-
-
-
-
?
cefazolin + H2O
(2R)-2-[(R)-carboxy[(1H-tetrazol-1-ylacetyl)amino]methyl]-5-[[(5-methyl-1,3,4-thiadiazol-2-yl)sulfanyl]methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
show the reaction diagram
cefcapene + H2O
(2R)-2-[(R)-{[(2Z)-2-(2-amino-1,3-thiazol-4-yl)pent-2-enoyl]amino}(carboxy)methyl]-5-[(carbamoyloxy)methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
show the reaction diagram
-
-
-
-
?
cefdinir + H2O
(2R)-2-[(R)-{[(2Z)-2-(2-amino-1,3-thiazol-4-yl)-2-(hydroxyimino)acetyl]amino}(carboxy)methyl]-5-ethenyl-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
show the reaction diagram
-
-
-
-
?
cefepime + H2O
(2R)-2-[(R)-[[(2Z)-2-(2-amino-1,3-thiazol-4-yl)-2-(methoxyimino)acetyl]amino](carboxy)methyl]-5-[(1-methylpyrrolidinium-1-yl)methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylate
show the reaction diagram
cefixime + H2O
?
show the reaction diagram
-
-
-
-
?
cefotaxime + H2O
(2R)-5-[(acetyloxy)methyl]-2-[(R)-[[(2E)-2-(2-amino-1,3-thiazol-4-yl)-2-(methoxyimino)acetyl]amino](carboxy)methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
show the reaction diagram
cefoxitin + H2O
(2R)-5-[(carbamoyloxy)methyl]-2-[(S)-carboxy(methoxy)[(thiophen-2-ylacetyl)amino]methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
show the reaction diagram
cefoxitin + H2O
(2R)-5-[(carbamoyloxy)methyl]-2-[(S)-carboxy(methoxy)[2-(thiophen-2-yl)acetamido]methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
show the reaction diagram
low activity
-
-
?
cefpirome + H2O
(2S)-2-[(R)-{[(2Z)-2-(2-amino-1,3-thiazol-4-yl)-2-(methoxyimino)acetyl]amino}(carboxy)methyl]-5-[(6,7-dihydro-5H-cyclopenta[b]pyridin-1-ium-1-yl)methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylate
show the reaction diagram
-
-
-
?
cefpodoxime + H2O
(2R)-2-[(R)-{[(2Z)-2-(2-amino-1,3-thiazol-4-yl)-2-(methoxyimino)acetyl]amino}(carboxy)methyl]-5-(methoxymethyl)-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
show the reaction diagram
-
-
-
-
?
ceftazidime + H2O
(2R)-2-[(R)-[[(2Z)-2-(2-amino-1,3-thiazol-4-yl)-2-[[(2-carboxypropan-2-yl)oxy]imino]acetyl]amino](carboxy)methyl]-5-[(pyridin-1-ium-1-yl)methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylate
show the reaction diagram
low activity
-
-
?
ceftazidime + H2O
(2R)-2-[(R)-{[(2Z)-2-(2-amino-1,3-thiazol-4-yl)-2-{[(2-carboxypropan-2-yl)oxy]imino}acetyl]amino}(carboxy)methyl]-5-[(pyridin-1-ium-1-yl)methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylate
show the reaction diagram
ceftazidime + H2O
?
show the reaction diagram
-
-
-
-
?
ceftizoxime + H2O
(2R)-2-[(R)-{[(2Z)-2-(2-amino-1,3-thiazol-4-yl)-2-(methoxyimino)acetyl]amino}(carboxy)methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
show the reaction diagram
-
-
-
-
?
ceftizoxime + H2O
?
show the reaction diagram
-
-
-
-
?
ceftriaxone + H2O
?
show the reaction diagram
-
-
-
-
?
cefuroxime + H2O
(2R)-5-[(carbamoyloxy)methyl]-2-[(R)-carboxy{[(2Z)-2-(furan-2-yl)-2-(methoxyimino)acetyl]amino}methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
show the reaction diagram
CENTA + H2O
(2R)-5-{[(3-carboxy-4-nitrophenyl)sulfanyl]methyl}-2-{(R)-carboxy[2-(thiophen-2-yl)acetamido]methyl}-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
show the reaction diagram
-
-
-
-
?
CENTA + H2O
?
show the reaction diagram
commercial chromogenic substrate
-
-
?
cephalexin + H2O
(2R)-2-[(R)-[[(2R)-2-amino-2-phenylacetyl]amino](carboxy)methyl]-5-methyl-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
show the reaction diagram
cephaloglycin + H2O
(2R)-5-[(acetyloxy)methyl]-2-[(R)-{[(2R)-2-amino-2-phenylacetyl]amino}(carboxy)methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
show the reaction diagram
-
-
-
-
?
cephaloridine + H2O
(2R)-2-[(R)-carboxy[(thiophen-2-ylacetyl)amino]methyl]-5-(pyridinium-1-ylmethyl)-3,6-dihydro-2H-1,3-thiazine-4-carboxylate
show the reaction diagram
cephalosporin + H2O
?
show the reaction diagram
cephalosporin C + H2O
N6-[(R)-{(2R)-5-[(acetyloxy)methyl]-4-carboxy-3,6-dihydro-2H-1,3-thiazin-2-yl}(carboxy)methyl]-6-oxo-D-lysine
show the reaction diagram
-
-
-
-
?
cephalothin + H2O
(2R)-5-[(acetyloxy)methyl]-2-[(R)-carboxy[(thiophen-2-ylacetyl)amino]methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
show the reaction diagram
cephalotin + H2O
(2R)-5-[(acetyloxy)methyl]-2-[(R)-carboxy[(thiophen-2-ylacetyl)amino]methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
show the reaction diagram
-
-
-
-
?
ciprofloxacin + H2O
?
show the reaction diagram
-
-
-
-
?
cloxacillin + H2O
(2R,4S)-2-[(R)-carboxy{[3-(2-chlorophenyl)-5-methyl-1,2-oxazole-4-carbonyl]amino}methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
show the reaction diagram
colistin + H2O
?
show the reaction diagram
-
-
-
-
?
doripenem + H2O
(4R,5S)-5-[(1S,2R)-1-carboxy-2-hydroxypropyl]-4-methyl-3-([(3S,5S)-5-[(sulfamoylamino)methyl]pyrrolidin-3-yl]sulfanyl)-4,5-dihydro-1H-pyrrole-2-carboxylic acid
show the reaction diagram
-
-
-
?
doripenem + H2O
(4R,5S)-5-[(1S,2R)-1-carboxy-2-hydroxypropyl]-4-methyl-3-({(3S,5S)-5-[(sulfamoylamino)methyl]pyrrolidin-3-yl}sulfanyl)-4,5-dihydro-1H-pyrrole-2-carboxylic acid
show the reaction diagram
-
-
-
-
?
gentamicin + H2O
?
show the reaction diagram
-
-
-
-
?
imipenem + H2O
(5R)-3-[[2-(carbonoimidoylamino)ethyl]sulfanyl]-5-[(1S,2R)-1-carboxy-2-hydroxypropyl]-4,5-dihydro-1H-pyrrole-2-carboxylic acid
show the reaction diagram
-
-
-
-
?
imipenem + H2O
(5R)-5-[(1S,2R)-1-carboxy-2-hydroxypropyl]-3-([2-[(iminomethyl)amino]ethyl]sulfanyl)-4,5-dihydro-1H-pyrrole-2-carboxylic acid
show the reaction diagram
-
-
-
?
imipenem + H2O
(5R)-5-[(1S,2R)-1-carboxy-2-hydroxypropyl]-3-({2-[(iminomethyl)amino]ethyl}sulfanyl)-4,5-dihydro-1H-pyrrole-2-carboxylic acid
show the reaction diagram
meropenem + H2O
(4R,5S)-5-[(1S,2R)-1-carboxy-2-hydroxypropyl]-3-[[(3S,5S)-5-(dimethylcarbamoyl)pyrrolidin-3-yl]sulfanyl]-4-methyl-4,5-dihydro-1H-pyrrole-2-carboxylic acid
show the reaction diagram
meropenem + H2O
(4R,5S)-5-[(1S,2R)-1-carboxy-2-hydroxypropyl]-3-{[(3S,5S)-5-(dimethylcarbamoyl)pyrrolidin-3-yl]sulfanyl}-4-methyl-4,5-dihydro-1H-pyrrole-2-carboxylic acid
show the reaction diagram
-
-
-
-
?
moxalactam + H2O
(2R)-2-{(R)-carboxy[2-carboxy(4-hydroxyphenyl)acetamido]methoxymethyl}-5-{[(1-methyl-1H-tetrazol-5-yl)sulfanyl]methyl}-3,6-dihydro-2H-1,3-oxazine-4-carboxylic acid
show the reaction diagram
-
-
-
-
?
nitrocefin + H2O
(2R)-2-[(R)-carboxy[2-(thiophen-2-yl)acetamido]methyl]-5-[(E)-2-(2,4-dinitrophenyl)ethenyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
show the reaction diagram
nitrocefin + H2O
(2R)-2-{(R)-carboxy[2-(thiophen-2-yl)acetamido]methyl}-5-[(E)-2-(2,4-dinitrophenyl)ethenyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
show the reaction diagram
oxacillin + H2O
(2R,4S)-2-{(R)-carboxy[(5-methyl-3-phenyl-1,2-oxazole-4-carbonyl)amino]methyl}-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
show the reaction diagram
penicillin G + H2O
(2R,4S)-2-[(R)-carboxy[(phenylacetyl)amino]methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
show the reaction diagram
phenoxymethylpenicillin + H2O
(2R,4S)-2-[(R)-carboxy(2-phenoxyacetamido)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
show the reaction diagram
-
-
-
-
?
piperacillin + H2O
(2R,4S)-2-[(R)-carboxy([(2R)-2-[(4-ethyl-2,3-dioxopiperazine-1-carbonyl)amino]-2-phenylacetyl]amino)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
show the reaction diagram
-
-
-
-
?
piperacillin + H2O
(2R,4S)-2-[(R)-carboxy[[(2R)-2-[[(4-ethyl-2,3-dioxopiperazin-1-yl)carbonyl]amino]-2-phenylacetyl]amino]methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
show the reaction diagram
-
-
-
-
?
sulbactam + H2O
(2R,4S)-2-(carboxymethyl)-5,5-dimethyl-1,1-dioxo-1lambda~6~,3-thiazolidine-4-carboxylic acid
show the reaction diagram
-
-
-
-
?
ticarcillin + H2O
(2R,4S)-2-[(R)-carboxy[[(2R)-2-carboxy-2-(thiophen-3-yl)acetyl]amino]methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
show the reaction diagram
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
amikacin + H2O
?
show the reaction diagram
-
-
-
-
?
amoxicillin + H2O
(2R,4S)-2-[(R)-[[(2R)-2-amino-2-(4-hydroxyphenyl)acetyl]amino](carboxy)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
show the reaction diagram
-
-
-
-
?
ampicillin + H2O
(2R,4S)-2-[(R)-[[(2R)-2-amino-2-phenylacetyl]amino](carboxy)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
show the reaction diagram
-
-
-
-
?
benzylpenicillin + H2O
(2R,4S)-2-[(R)-carboxy(2-phenylacetamido)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
show the reaction diagram
-
-
-
-
?
carbapenem + H2O
[(2R)-2,3-dihydro-1H-pyrrol-2-yl]acetic acid
show the reaction diagram
-
-
-
-
?
cefepime + H2O
(2R)-2-[(R)-[[(2Z)-2-(2-amino-1,3-thiazol-4-yl)-2-(methoxyimino)acetyl]amino](carboxy)methyl]-5-[(1-methylpyrrolidinium-1-yl)methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylate
show the reaction diagram
-
-
-
-
?
cefixime + H2O
?
show the reaction diagram
-
-
-
-
?
cefotaxime + H2O
(2R)-5-[(acetyloxy)methyl]-2-[(R)-[[(2E)-2-(2-amino-1,3-thiazol-4-yl)-2-(methoxyimino)acetyl]amino](carboxy)methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
show the reaction diagram
-
-
-
-
?
ceftazidime + H2O
?
show the reaction diagram
-
-
-
-
?
ceftizoxime + H2O
?
show the reaction diagram
-
-
-
-
?
ceftriaxone + H2O
?
show the reaction diagram
-
-
-
-
?
cephalosporin + H2O
?
show the reaction diagram
-
the enzyme is responsible for the resistance to extended spectrum cephalosporins
-
-
?
ciprofloxacin + H2O
?
show the reaction diagram
-
-
-
-
?
colistin + H2O
?
show the reaction diagram
-
-
-
-
?
gentamicin + H2O
?
show the reaction diagram
-
-
-
-
?
imipenem + H2O
(5R)-3-[[2-(carbonoimidoylamino)ethyl]sulfanyl]-5-[(1S,2R)-1-carboxy-2-hydroxypropyl]-4,5-dihydro-1H-pyrrole-2-carboxylic acid
show the reaction diagram
-
-
-
-
?
meropenem + H2O
(4R,5S)-5-[(1S,2R)-1-carboxy-2-hydroxypropyl]-3-[[(3S,5S)-5-(dimethylcarbamoyl)pyrrolidin-3-yl]sulfanyl]-4-methyl-4,5-dihydro-1H-pyrrole-2-carboxylic acid
show the reaction diagram
-
-
-
-
?
piperacillin + H2O
(2R,4S)-2-[(R)-carboxy([(2R)-2-[(4-ethyl-2,3-dioxopiperazine-1-carbonyl)amino]-2-phenylacetyl]amino)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
show the reaction diagram
-
-
-
-
?
additional information
?
-
-
substrate specificity in vivo with different enzymes genotypes, overview
-
-
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Cu2+
-
metalloenzyme
Ni2+
-
Ni2+ binds in the Zn2+-site and the ring-opened product coordinates Ni2+
additional information
-
the metal binding sites, particularly the Zn2 site, in metallo-beta-lactamase L1 are very flexible and can accommodate a number of different divalent metal ions
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
(R)-3-(N-benzyloxycarbonylamino)-2-oxo-butylphosphate
-
-
(RS)-4-(N-benzyloxycarbonyl)amino-3-oxo-2-butylphosphate
-
-
([(benzylsulfonyl)amino]methyl)boronic acid
-
([[(2-ethoxynaphthalen-1-yl)carbonyl]amino]methyl)boronic acid
-
3-(N-benzyloxycarbonyl)amino-2-oxopropylphenylphosphonate
-
-
3-(N-benzyloxycarbonyl)amino-2-oxopropylphosphate
-
-
3-(N-benzyloxycarbonyl)amino-2-oxopropylphosphonate
-
-
3-aminophenyl boronic acid
-
plasmid-encoded, pBC1e, beta-lactamase ACT-1
3-[(2R)-2-(dihydroxyboranyl)-2-[[(thiophen-2-ylmethyl)sulfonyl]amino]ethyl]benzoic acid
-
3-[(2R)-2-[(benzylsulfonyl)amino]-2-(dihydroxyboranyl)ethyl]benzoic acid
-
4-(N-benzyloxycarbonyl)amino-3-oxobutylphosphonate
-
-
4-([[(dihydroxyboranyl)methyl]sulfamoyl]methyl)benzoic acid
-
6-beta-iodopenicillanic acid
-
enzyme 2 OXA2
AVE1330A
-
IC50: 8 nM
avibactam
-
-
aztreonam
BAL29880
-
-
BAL30072
-
-
beta-lactamase inhibitor protein
i.e. BLIP, 17 kDa protein produced by Streptomyces clavuligerus, specific for class A enzymes, construction of diverse mutants of BLIP for identification of functional epitopes, enzyme-inhibitor complex modeling
-
beta-lactamase inhibitory protein
i.e. BLIP. Structures of two thermodynamically distinctive complexes of BLIP mutants with TEM-1 beta-lactamase. The complex BLIP Y51ATEM-1 is a tight binding complex with the most negative binding heat capacity change among all of the mutants, whereas BLIP W150ATEM-1 is a weak complex with one of the least negative binding heat capacity changes. BLIP Tyr51 is a canonical and Trp150 an anti-canonical TEM-1-contact residue (canonical refers to the alanine substitution resulting in a matched change in the hydrophobicity of binding free energy). Structure determination indicates a rearrangement of the interactions between Asp49 of the W150A BLIP mutant and the catalytic pocket of TEM-1. The Asp49 of W150A moves more than 4 A to form two new hydrogen bonds while losing four original hydrogen bonds
-
cefotaxime
-
-
cefpodoxime
-
-
ceftriaxone
-
-
clavulanic acid
Cloxacillin
-
-
Co2+
-
poor inhibition
doripenem
-
-
ertapenem
-
-
ethyl 3-(benzyloxycarbonyl)amino-2-oxo-1,1-difluoropropylphosphonate
-
-
HSAYSDTRRGDYG
-
synthetic peptide, derived from screens using phage display and peptide arrays
Imipenem
meropenem
-
-
methyl 3-(N-benzyloxycarbonyl)amino-2-oxo-1-propylphosphate
-
-
MK-7655
-
-
moxalactam
N-[N'-(benzyloxycarbonyl)aminoacetyl]amino-methylphosphonate
-
-
p-chloromercuribenzoate
-
-
p-chloromercuriphenylsulfonate
-
-
penem 1
a 6-methylidene penem, proposed mechanism for penem 1 and OXA-1, overview. Penem 1 can also cause the essentially irreversible decarboxylation of OXA-1
penem 3
a 6-methylidene penem
phenyl 3-(N-benzyloxycarbonyl)amino-2-oxopropylphosphate
-
-
phenyl 3-(N-benzyloxycarbonyl)amino-2-oxopropylphosphonate
-
-
RPX7009
-
-
RRGHYY
SA-1-204
a penam sulfone inhibitor
sodium benzyl (2-hydroxy-2-phenylethyl)phosphonate
-
sodium benzyl (2-oxo-2-phenylethyl)phosphonate
-
sodium benzyl 2-(1',3'-benzothiazol-2'-yl)-2-oxo-ethylphosphonate
-
sodium benzyl [2-(biphenyl-4-yl)-2-hydroxyethyl]phosphonate
-
sodium benzyl [2-(biphenyl-4-yl)-2-oxoethyl]phosphonate
-
sodium benzyl [2-oxo-2-(2-oxo-2,3-dihydro-1,3-benzoxazol-6-yl)ethyl]phosphonate
-
sodium benzyl {2-[3-(2-chlorophenyl)-5-methyl-1,2-oxazol-4-yl]-2-oxoethyl}phosphonate
-
sodium biphenyl-4-ylmethyl (2-oxo-2-phenylethyl)phosphonate
-
sodium biphenyl-4-ylmethyl [2-(biphenyl-4-yl)-2-oxoethyl]phosphonate
-
sodium phenyl (2-oxo-2-phenylethyl)phosphonate
-
sodium phenyl [2-(biphenyl-4-yl)-2-oxoethyl]phosphonate
-
sodium phenyl [2-oxo-2-(pentafluorophenyl)ethyl]phosphonate
-
Sulbactam
tazobactam
vanadate/(3,4-dihydroxyphenyl)methanaminium complex
-
competitive inhibition, 1:1 complexes of vanadate with a variety of catechols
vanadate/2,3,5,6-tetrahydroxycyclohexa-2,5-diene-1,4-dione complex
-
competitive inhibition, 1:1 complexes of vanadate with a variety of catechols
vanadate/2,3-dihydroxynaphthalene-1,4-dione complex
-
competitive inhibition, 1:1 complexes of vanadate with a variety of catechols
vanadate/2-(3,4-dihydroxyphenyl)acetate complex
-
competitive inhibition, 1:1 complexes of vanadate with a variety of catechols
vanadate/2-methoxyphenol complex
-
competitive inhibition, 1:1 complexes of vanadate with a variety of catechols
vanadate/3,4,5,6-tetrafluorobenzene-1,2-diol complex
-
competitive inhibition, 1:1 complexes of vanadate with a variety of catechols
vanadate/3,4-dihydroxybenzoate complex
-
competitive inhibition, 1:1 complexes of vanadate with a variety of catechols
vanadate/3-phenylcatechol complex
-
competitive inhibition, 1:1 complexes of vanadate with a variety of catechols, most effective
vanadate/4-nitrobenzene-1,2-diol complex
-
competitive inhibition, 1:1 complexes of vanadate with a variety of catechols
vanadate/biphenyl-3,4-diol complex
-
competitive inhibition, 1:1 complexes of vanadate with a variety of catechols
vanadate/naphthalene-1,2-diol complex
-
competitive inhibition, 1:1 complexes of vanadate with a variety of catechols
vanadate/naphthalene-2,3-diol complex
-
competitive inhibition, 1:1 complexes of vanadate with a variety of catechols
vanadate/phenol complex
-
competitive inhibition, 1:1 complexes of vanadate with a variety of catechols
vanadate/pyrocatechol complex
-
competitive inhibition, 1:1 complexes of vanadate with a variety of catechols
additional information
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0023
(2S,5R,6R)-6-[[(2R)-2-carboxy-2-thiophen-3-ylacetyl]amino]-3,3-dimethyl-7-oxo-4-thia-1-azabicyclo[3.2.0]heptane-2-carboxylic acid
beta-lactamases CTX-M-25
0.323
(6R,7R)-3-[(acetyloxy)methyl]-7-(formylamino)-8-oxo-5-thia-1-azabicyclo[4.2.0]oct-2-ene-2-carboxylate
-
pH and temperature not specified in the publication
0.06
(6R,7R)-3-[(acetyloxy)methyl]-7-[hydroxy(phenylacetyl)amino]-8-oxo-5-thia-1-azabicyclo[4.2.0]oct-2-ene-2-carboxylate
-
pH and temperature not specified in the publication
0.014
(6R,7R)-3-[(acetyloxy)methyl]-8-oxo-7-[(thiophen-2-ylacetyl)amino]-5-thia-1-azabicyclo[4.2.0]oct-2-ene-2-carboxylate
-
pH and temperature not specified in the publication
0.002 - 0.013
(6R,7S)-3-[(3-carboxy-4-nitro-phenyl)sulfanylmethyl]-8-oxo-7-[(2-thiophen-2-ylacetyl)amino]-5-thia-1-azabicyclo-[4.2.0]-oct-2-ene-2-carboxylic acid
0.35
6-aminopenicillanic acid
-
-
0.075
7-(thienyl-2-acetamido)-3-[2-(4-N,N-dimethylaminophenylazo)pyridinium-methyl]-3-cephem-4-carboxylic acid
-
-
0.22
amoxycillin
-
-
0.00016 - 0.455
ampicillin
0.000004 - 0.55
aztreonam
0.0004 - 0.155
benzylpenicillin
0.017
carbenicillin
-
-
0.008 - 0.091
cefaclor
0.096 - 0.125
cefaloridine
0.027
cefalothin
-
in 50 mM phosphate buffer (pH 7.0), at 30°C
0.005 - 0.433
cefalotin
0.054 - 0.43
cefazolin
0.025
cefcapene
-
in 50 mM phosphate buffer (pH 7.0), at 30°C
0.0008
cefdinir
-
in 50 mM phosphate buffer (pH 7.0), at 30°C
0.027 - 75
cefepime
0.000015 - 45
cefotaxime
0.0000011 - 1.5
cefoxitin
0.021
cefpirome
37°C, pH 7.0
0.0057 - 270
ceftazidime
0.0000012 - 0.242
cefuroxime
0.014 - 0.042
cephalexin
0.093 - 950
cephaloridine
0.95
cephalosporin C
-
-
0.0021 - 85
cephalothin
0.044 - 0.26
cephalotin
0.064 - 0.151
doripenem
0.00005 - 32
Imipenem
0.00011 - 0.119
meropenem
0.004 - 18
nitrocefin
0.0000006 - 0.0001
Oxacillin
0.022 - 0.278
penicillin G
0.02 - 0.54
piperacillin
0.00047 - 0.03
Sulbactam
0.665
ticarcillin
-
-
additional information
additional information
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
8.2
(2S,5R,6R)-6-[[(2R)-2-carboxy-2-thiophen-3-ylacetyl]amino]-3,3-dimethyl-7-oxo-4-thia-1-azabicyclo[3.2.0]heptane-2-carboxylic acid
beta-lactamases CTX-M-25
1.02
(6R,7R)-3-[(acetyloxy)methyl]-7-(formylamino)-8-oxo-5-thia-1-azabicyclo[4.2.0]oct-2-ene-2-carboxylate
-
pH and temperature not specified in the publication
0.121
(6R,7R)-3-[(acetyloxy)methyl]-7-[hydroxy(phenylacetyl)amino]-8-oxo-5-thia-1-azabicyclo[4.2.0]oct-2-ene-2-carboxylate
-
pH and temperature not specified in the publication
1.81
(6R,7R)-3-[(acetyloxy)methyl]-8-oxo-7-[(thiophen-2-ylacetyl)amino]-5-thia-1-azabicyclo[4.2.0]oct-2-ene-2-carboxylate
-
pH and temperature not specified in the publication
0.08 - 1.6
(6R,7S)-3-[(3-carboxy-4-nitro-phenyl)sulfanylmethyl]-8-oxo-7-[(2-thiophen-2-ylacetyl)amino]-5-thia-1-azabicyclo-[4.2.0]-oct-2-ene-2-carboxylic acid
659
6-aminopenicillanic acid
-
-
50
7-(thienyl-2-acetamido)-3-[2-(4-N,N-dimethylaminophenylazo)pyridinium-methyl]-3-cephem-4-carboxylic acid
-
-
910
amoxycillin
-
-
0.43 - 1375
ampicillin
0.4 - 84
aztreonam
13 - 1400
benzylpenicillin
32
carbenicillin
-
-
14 - 38
cefaclor
1020 - 1300
cefaloridine
510
cefalothin
-
in 50 mM phosphate buffer (pH 7.0), at 30°C
9 - 1800
cefalotin
325 - 560
cefazolin
110
cefcapene
-
in 50 mM phosphate buffer (pH 7.0), at 30°C
83
cefdinir
-
in 50 mM phosphate buffer (pH 7.0), at 30°C
0.008 - 34
cefepime
0.004 - 1400
cefotaxime
0.043 - 18
cefoxitin
1.5
cefpirome
37°C, pH 7.0
0.00833 - 33
ceftazidime
0.017 - 190
cefuroxime
55 - 115
cephalexin
50 - 780
cephaloridine
33
cephalosporin C
-
-
0.15 - 540
cephalothin
125 - 153
cephalotin
0.04 - 1032
doripenem
0.002 - 757
Imipenem
0.007 - 583
meropenem
3 - 2220
nitrocefin
0.009 - 0.18
Oxacillin
12.3 - 1570
penicillin G
39 - 940
piperacillin
4 - 20
Sulbactam
8.2 - 121
ticarcillin
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
3.16
(6R,7R)-3-[(acetyloxy)methyl]-7-(formylamino)-8-oxo-5-thia-1-azabicyclo[4.2.0]oct-2-ene-2-carboxylate
-
pH and temperature not specified in the publication
2.02
(6R,7R)-3-[(acetyloxy)methyl]-7-[hydroxy(phenylacetyl)amino]-8-oxo-5-thia-1-azabicyclo[4.2.0]oct-2-ene-2-carboxylate
-
pH and temperature not specified in the publication
85.1
(6R,7R)-3-[(acetyloxy)methyl]-8-oxo-7-[(thiophen-2-ylacetyl)amino]-5-thia-1-azabicyclo[4.2.0]oct-2-ene-2-carboxylate
-
pH and temperature not specified in the publication
1200 - 3000
ampicillin
1500 - 6100
cefalotin
130 - 220
cefoxitin
180 - 260
ceftazidime
1700 - 8600
doripenem
2200 - 9200
Imipenem
2600 - 7400
meropenem
3100 - 10900
nitrocefin
210 - 950
penicillin G
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.3 - 0.36
(R)-3-(N-benzyloxycarbonylamino)-2-oxo-butylphosphate
0.088 - 0.2
(RS)-4-(N-benzyloxycarbonyl)amino-3-oxo-2-butylphosphate
0.00007
([(benzylsulfonyl)amino]methyl)boronic acid
pH 6.5, 22°C
0.000033
([[(2-ethoxynaphthalen-1-yl)carbonyl]amino]methyl)boronic acid
pH 6.5, 22°C
0.15 - 0.19
3-(N-benzyloxycarbonyl)amino-2-oxopropylphenylphosphonate
0.1 - 0.6
3-(N-benzyloxycarbonyl)amino-2-oxopropylphosphate
0.15
3-(N-benzyloxycarbonyl)amino-2-oxopropylphosphonate
-
-
0.086
3-aminophenyl boronic acid
-
30°C, pH 7.0, plasmid-encoded, pBC1e, beta-lactamase ACT-1
0.000001
3-[(2R)-2-(dihydroxyboranyl)-2-[[(thiophen-2-ylmethyl)sulfonyl]amino]ethyl]benzoic acid
pH 6.5, 22°C
0.00043
3-[(2R)-2-[(benzylsulfonyl)amino]-2-(dihydroxyboranyl)ethyl]benzoic acid
pH 6.5, 22°C
0.47 - 0.6
4-(N-benzyloxycarbonyl)amino-3-oxobutylphosphonate
0.000025
4-([[(dihydroxyboranyl)methyl]sulfamoyl]methyl)benzoic acid
pH 6.5, 22°C
0.438
AAGHYY
-
pH 7.0
0.00004
aztreonam
-
pH 74, temperature not specified in the publication
0.009
BAL29880
-
pH 74, temperature not specified in the publication
0.0007
BAL30072
-
pH 74, temperature not specified in the publication
0.0000005
beta-lactamase inhibitor protein
wild-type inhibitor protein, pH 7.5, 25°C
-
0.32
clavulanic acid
37°C, pH 7.0
0.0023
doripenem
-
pH 74, temperature not specified in the publication
0.00028
ertapenem
-
pH 74, temperature not specified in the publication
0.93
ethyl 3-(benzyloxycarbonyl)amino-2-oxo-1,1-difluoropropylphosphonate
-
-
0.298
HSAYSDTRRGDYG
-
pH 7.0
0.0011
Imipenem
-
pH 74, temperature not specified in the publication
0.00027
meropenem
-
pH 74, temperature not specified in the publication
0.24
methyl 3-(N-benzyloxycarbonyl)amino-2-oxo-1-propylphosphate
-
-
0.014
moxalactam
-
-
0.43
N-[N'-(benzyloxycarbonyl)aminoacetyl]amino-methylphosphonate
-
-
0.079 - 0.146
nitrocefin
0.00005
penem 1
pH 7.2, temperature not specified in the publication, recombinant enzyme
0.00038
penem 3
pH 7.2, temperature not specified in the publication, recombinant enzyme
0.11 - 0.13
phenyl 3-(N-benzyloxycarbonyl)amino-2-oxopropylphosphate
0.077 - 0.13
phenyl 3-(N-benzyloxycarbonyl)amino-2-oxopropylphosphonate
0.136
RRGHYY
-
pH 7.0
0.44 - 1
sodium benzyl (2-hydroxy-2-phenylethyl)phosphonate
0.15 - 1
sodium benzyl (2-oxo-2-phenylethyl)phosphonate
0.17 - 3600
sodium benzyl 2-(1',3'-benzothiazol-2'-yl)-2-oxo-ethylphosphonate
0.3 - 1
sodium benzyl [2-(biphenyl-4-yl)-2-hydroxyethyl]phosphonate
0.23 - 1
sodium benzyl [2-(biphenyl-4-yl)-2-oxoethyl]phosphonate
0.27 - 1.5
sodium benzyl [2-oxo-2-(2-oxo-2,3-dihydro-1,3-benzoxazol-6-yl)ethyl]phosphonate
0.43 - 1
sodium benzyl {2-[3-(2-chlorophenyl)-5-methyl-1,2-oxazol-4-yl]-2-oxoethyl}phosphonate
0.2 - 1
sodium biphenyl-4-ylmethyl (2-oxo-2-phenylethyl)phosphonate
0.006 - 0.2
sodium biphenyl-4-ylmethyl [2-(biphenyl-4-yl)-2-oxoethyl]phosphonate
1 - 1.05
sodium phenyl (2-oxo-2-phenylethyl)phosphonate
0.14 - 0.92
sodium phenyl [2-(biphenyl-4-yl)-2-oxoethyl]phosphonate
0.38 - 1
sodium phenyl [2-oxo-2-(pentafluorophenyl)ethyl]phosphonate
0.0092
Sulbactam
37°C, pH 7.0
0.0087
tazobactam
37°C, pH 7.0
0.045
vanadate/(3,4-dihydroxyphenyl)methanaminium complex
-
pH 7.0, 25°C
0.14
vanadate/2-(3,4-dihydroxyphenyl)acetate complex
-
pH 7.0, 25°C
0.2
vanadate/3,4-dihydroxybenzoate complex
-
pH 7.0, 25°C
0.003 - 0.023
vanadate/3-phenylcatechol complex
0.16
vanadate/4-nitrobenzene-1,2-diol complex
-
pH 7.0, 25°C
0.0011 - 0.03
vanadate/biphenyl-3,4-diol complex
0.016 - 0.077
vanadate/naphthalene-2,3-diol complex
0.0015 - 0.062
vanadate/pyrocatechol complex
additional information
additional information
-
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.000008
AVE1330A
Escherichia coli
-
IC50: 8 nM
0.00013
clavulanic acid
Escherichia coli
-
IC50: 130 nM
0.00003
penem 1
Escherichia coli
pH 7.2, temperature not specified in the publication, recombinant enzyme
0.00006
penem 3
Escherichia coli
pH 7.2, temperature not specified in the publication, recombinant enzyme
0.00004
tazobactam
Escherichia coli
-
IC50: 40 nM
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
13
-
enzyme OXA1
250
-
enzyme OXA2
41
-
enzyme PSE2
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.5
isoelectric focusing, beta-lactamases CTX-M-25, pH-range 3.5-9.5
8.2
isoelectric focusing
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
UniProt
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
extended-spectrum beta-lactamases (ESBL)-producing Enterobacteriaceae from spring waters can be a thread to human health. ESBL-producing Enterobacteriaceae were found in four out of 50 sampled spring waters (4/50, 8.0%) and a total of 16 non-duplicate ESBL-producing Enterobacteriaceae are obtained, including 13 Escherichia coli and three Klebsiella pneumoniae strains. All 16 nonduplicate ESBL-producing Enterobacteriaceae isolates harbour genes encoding CTX-M ESBLs, among which six expressed CTX-M-15, five produced CTX-M-14, three produced CTX-M-55 and two expressed CTX-M-27. Four multilocus sequence types (ST) are found and ST131 is the dominant type (8/16, 50.0%). The contamination of ESBL-producing Enterobacteriaceae are present in spring waters of Mountain Tai
evolution
malfunction
while point mutations in the PWP triad preserve the overall secondary structures around the allosteric site, they result in a more open and dynamic global structure with decreased chemical stability and increased aggregation propensity. These mutant enzymes with a less compact hydrophobic core around the allosteric site display significant activity loss
additional information
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
Q840M4_ECOLX
291
0
30921
TrEMBL
-
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
24600
-
enzyme 1, OXA1, gel filtration
26000
-
disc electophoresis
27970
-
mass spectrum analysis
28000
SDS-PAGE
28200
-
1 * 28200, SDS-PAGE
29000
x * 29000, beta-lactamases CTX-M-25, SDS-PAGE
30000
-
SDS-PAGE
35000
-
enzyme 3, PSE2, gel fitration
40000
SDS-PAGE
50600
-
enzyme 2, OXA2, gel fitration
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
additional information
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
0.98 mg/ml purified mutant N152A in complex with inhibitor moxalactam in 1.7 M potassium phosphate, pH 8.7, 23°C, after microseeding with the wild-type enzyme in 1 M potassium phosphate, pH 8.7, vapor diffusion hanging drop method, serial dilutions, 5-7 days, X-ray diffraction structure determination and analysis at 1.83 A resolution
2.5-3 mg/ml purified recombinant enzyme in 10% PEG 8000, 0.05 M HEPES, pH 7.5, vapour diffusion sitting drop method, equilibration of 0.01 ml protein solution over a reservoir solution containing 20% PEG 8000, macro-seeding at 1.2-1.5 mg/ml, growth of prismatic crystals, X-ray diffraction structure determination and analysis at 1.5 A resolution, modeling
-
crystal quality of Toho-1 is improved by using surface modification to remove a sulfate ion involved in crystal packing
in complex with ([(benzylsulfonyl)amino]methyl)boronic acid, 4-([[(dihydroxyboranyl)methyl]sulfamoyl]methyl)benzoic acid, and 3-[(2R)-2-[(benzylsulfonyl)amino]-2-(dihydroxyboranyl)ethyl]benzoic acid, to 1.6, 1.8 and 1.6 A resolution, respectively. The sulfonamides have a highly distinct structure-activity relationship from the carboxamides, with high ligand efficiencies, and Ki values down to 25 nM and up to 23 times better for smaller analogs. Conversely, Ki values are 10 to 20 times worse for larger molecules than in the carboxamide congener series. X-ray crystal structures suggest that this altered structure-activity relationship results from the different geometry and polarity of the sulfonamide versus the carboxamide
microseeding, enzyme/beta-lactamase inhibitory protein(BLIP) complexes: BLIP/TEM-1, BLIP(W150A)/TEM-1 and BLIP(Y51A)/TEM-1
purified recombinant enzyme, hanging drop vapor diffusion method, mixing of 9 mg/ml protein solution with crystallization solution containing 0.05 M HEPES, pH 7.5, and 15% PEG 8000, X-ray diffraction structure determination and analysis
three-dimensional analysis using crystal structure PDB ID 1IYO, modeling
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
A233V
naturally occuring genetic variant
D130G/M154L
naturally occuring genetic variation
D130N/M154L
naturally occuring genetic variation
D179G
-
activity unchanged or enhanced
D179N
-
activity unchanged or enhanced
D66A
site-saturation mutagenesis at position 66, 8fold increase in minimum inhibitory concentration for ceftazidime compared with the wild type (0.25 to 2 microg/ml). Mutation results in only minor changes in steady-state protein levels
D66C
site-saturation mutagenesis at position 66. Expression of this variant is diminished relative to that of the other proteins
D66L
site-saturation mutagenesis at position 66, rise in resistance against ceftazidime compared with the wild type
D66M
site-saturation mutagenesis at position 66, rise in resistance against ceftazidime compared with the wild type. Mutation results in only minor changes in steady-state protein levels
D66N
site-saturation mutagenesis at position 66, mutation leads to a moderate enhancement of extended-spectrum cephalosporin resistance and an increase in cefepime and cefotaxime resistance. Mutation results in only minor changes in steady-state protein levels
D66P
site-saturation mutagenesis at position 66
D66W
site-saturation mutagenesis at position 66, mutation results in only minor changes in steady-state protein levels
D66Y
site-saturation mutagenesis at position 66, mutation results in only minor changes in steady-state protein levels
D95N
naturally occuring genetic variation
E104K
-
E104M increased kcat
E104K/G238S
-
-
E104M/G238S
-
E104M/G238S 1000 fold higher hydrolysis of cefotaxime
M154L
naturally occuring genetic variation
M154L/G222D
naturally occuring genetic variation
M182T/T195S/A224V
-
mutant selected by a directed evolution strategy. It is allosterically downregulated by Zn2+, Ni2+ and Co2+ with binding affinities around 300 microM
N152A
site-directed mutagenesis, 6300fold reduced kinetic efficiency compared to the wild-type enzyme
P226A
site-directed mutagenesis, the mutant has 92% reduced activity compared to wild-type
P252A
site-directed mutagenesis, the mutant has 85% reduced activity compared to wild-type
R164N
-
activity unchanged or enhanced
R164S
-
activity unchanged or enhanced
R274N/R276N
sitting-drop vapour-diffusion technique, surface-modified Toho-1 variant does not form merohedrally twinned crystals. Crystals diffract to a significantly higher resolution (0.97 A) than the wild-type crystals (1.65 A)
R276C
site-directed mutagenesis, the MICs of cefotaxime are clearly lower, clearly reduced catalytic efficiency towards cefotaxime. Investigation of the role of Arg276 in cefotaxime hydrolysis
R276G
site-directed mutagenesis, the MICs of cefotaxime are clearly lower, clearly reduced catalytic efficiency towards cefotaxime. Investigation of the role of Arg276 in cefotaxime hydrolysis
R276H
site-directed mutagenesis, investigation of the role of Arg276 in cefotaxime hydrolysis
R276N
site-directed mutagenesis, investigation of the role of Arg276 in cefotaxime hydrolysis
R276S
site-directed mutagenesis, the MICs of cefotaxime are clearly lower, clearly reduced catalytic efficiency towards cefotaxime. Investigation of the role of Arg276 in cefotaxime hydrolysis
R276W
site-directed mutagenesis, the MICs of cefotaxime are clearly lower, clearly reduced catalytic efficiency towards cefotaxime. Investigation of the role of Arg276 in cefotaxime hydrolysis
R61H/E64H/43H
-
circularly permuted enzyme, created by rational design. Mutant shows little regulation upon metal ion binding except for a weak activation with Zn2+
S287N
the AmpC variants AmpC-A and AmpC-B2 harboring the S287N substitution are obtained by mutagenesis from cephalosporinases representative of the phylogenetic groups A and B2 of Escherichia coli. Their biochemical characterization reveals that the S287N replacement leads to an important increase in the catalytic efficiency toward extended-spectrum cephalosporins in the AmpC beta-lactamase of group A only
V88L/M154L
naturally occuring genetic variation
W229A
site-directed mutagenesis, the mutant has 98% reduced activity compared to wild-type
W229F
site-directed mutagenesis, the mutant has 84% reduced activity compared to wild-type
W229Y
site-directed mutagenesis, the mutant has 82% reduced activity compared to wild-type
W290F
-
activity and spectroscopic properties of the mutant enzyme does not differ significantly from those of the wild type, indicating that the mutation has only a very limited effect on the structure of the protein. The stability of the folded protein is reduced, however, by 5-10 kJ mol-1 relative to that of the molten globule intermediate (H), but the values of the folding rate constants are unchanged, suggesting that Trp290 becomes organized in its native like environment only after the rate-limiting step, i.e., the C-terminal region of the enzyme folds very late
additional information
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
48
the wild-type Tm is around 48°C occurring over a temperature range of about 23°C (35-58°C) for both the wild-type and the three W229 mutants
55.1
melting temperature of the purified NDM-1 variant
60
-
1% activity after 5 min
61.4
melting temperature of the purified NDM-1 variant
63.4
melting temperature of the purified NDM-1 variant
64.6
melting temperature of the purified NDM-1 variant
72.1
melting temperature of the purified NDM-1 variant
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
2°C, 0.1 M Na2HPO4/KH2PO4, pH 7.0, slow loss of activity
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
beta-lactamases CTX-M-25
CM-Sepharose column chromatography
-
CTX-M-1 wild-type and six derived mutants are purified by affinity chromatography
recombinant His-tagged wild-type and mutant enzymes from Escherichia coli strain BL21(DE3) by nickel affinity chromatography
recombinant N-terminally His6-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography, cleavage of the N-terminal His6-tag using recombinant human Rhinovirus 3C protease, and further purification of the untagged protein by affinity chromatography, followed by ultrafiltration
wild type OXA-1 purified by CM-cellulose chromatography and His6-tagged wild type OXA-1 purified by nickel-affinity chromatography
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene blaCTX-M-27, extended-spectrum beta-lactamases (ESBL), genotyping
beta-lactamases CTX-M-25
diverse multidrug resistant extended-spectrum beta-lactamase-producing Escherichia coli strains among uropathogens of pediatrics in north of Iran are isolated and tested by PCR for the presence or absence of CTX, TEM, SHV, GES, and VEB beta-lactamase genes, genotyping
-
expressed in Escherichia coli
expressed in Escherichia coli BL21(DE3) cells
-
expressed in Escherichia coli DH10B
expressed in Escherichia coli TG1
gene blaCMY-2, DNA and amino acid sequence determination and analysis, genotyping of the bla gene in 14 pAmpC-producing Escherichia coli strains, 11 sequence types are found, genomic relationships analysis
gene blaCTX-M-14, extended-spectrum beta-lactamases (ESBL), genotyping
gene blaCTX-M-15, extended-spectrum beta-lactamases (ESBL), genotyping
gene blaCTX-M-55, extended-spectrum beta-lactamases (ESBL), genotyping
gene blaFOX-4, recombinant expression in Escherichia coli strain BL21(DE3)
-
gene blaNDM-12, genotyping, recombinant expression of N-terminally His6-tagged enzyme in Escherichia coli strain BL21(DE3)
gene blaNDM-3, genotyping, recombinant expression of N-terminally His6-tagged enzyme in Escherichia coli strain BL21(DE3)
gene blaNDM-4, genotyping, recombinant expression of N-terminally His6-tagged enzyme in Escherichia coli strain BL21(DE3)
gene blaNDM-5, genotyping, recombinant expression of N-terminally His6-tagged enzyme in Escherichia coli strain BL21(DE3)
gene blaNDM-6, genotyping, recombinant expression of N-terminally His6-tagged enzyme in Escherichia coli strain BL21(DE3)
gene blaNDM-7, genotyping, recombinant expression of N-terminally His6-tagged enzyme in Escherichia coli strain BL21(DE3)
gene blaNDM-8, genotyping, recombinant expression of N-terminally His6-tagged enzyme in Escherichia coli strain BL21(DE3)
gene blaOXA-1, recombinant expression in Escerichia coli strain BL21(DE3)
gene blaTEM-1, recombinant expression of His-tagged wild-type and mutant enzymes in Escherichia coli strain BL21(DE3)
genotyping and phenotyping of Escherichia coli strains with beta-lactamase activity in faeces from ducks
-
subcloning
-
RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
refolding of recombinant enzyme from periplasmic protein pellets by resuspension in 5 mL 50 mM Tris buffer, pH 7.8, with addition pf 10 ml 8 M urea
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
drug development
the PWP triad is an evolutionarily conserved motif unique to class A beta-lactamases aligning its allosteric site and hence is an effective potential target for enzyme regulation and selective drug design
pharmacology
-
enzyme is a target for design of non-beta-lactam, broad-spectrum peptidomimetic enzyme inhibitors
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Ambler, R.P.; Scott, G.K.
Partial amino acid sequence of penicillinase coded by Escherichia coli plasmid R6K
Proc. Natl. Acad. Sci. USA
75
3732-3736
1978
Escherichia coli, Escherichia coli W3310
Manually annotated by BRENDA team
Richmond, M.H.
beta-Lactamase (Escherichia coli) R+TEM
Methods Enzymol.
43
672-677
1975
Escherichia coli
Manually annotated by BRENDA team
Richmond, M.H.
Immunological techniques for studying beta-lactamases
Methods Enzymol.
43
86-100
1975
Escherichia coli, Staphylococcus aureus
Manually annotated by BRENDA team
Ogawara, H.; Maeda, K.; Umezawa, H.
A beta-lactamase of Escherichia coli
Biochim. Biophys. Acta
289
203-211
1972
Escherichia coli
Manually annotated by BRENDA team
Citri, N.
Penicillinase and other beta-lactamases
The Enzymes, 3rd Ed. (Boyer, P. D. , ed. )
4
23-46
1971
Enterobacter cloacae, Bacillus cereus, Bacillus licheniformis, Escherichia coli, Staphylococcus aureus
-
Manually annotated by BRENDA team
Ben-Mahrez, K.; Limam, F.; Bellaaj, A.; Rejiba, S.; Ben-Hamouda, T.; Alfeddy, N.; Belhadj, C.; Belhadj, O.
Purification and biochemical properties of beta-lactamase from Escherichia coli
J. Toxicol. Toxin Rev.
18
221-228
1999
Escherichia coli
-
Manually annotated by BRENDA team
Vakulenko, S.B.; Taibi-Tronche, P.; Toth, M.; Massova, I.; Lerner, S.A.; Mobashery, S.
Effects on substrate profile by mutational substitutions at position 164 and 179 of the class A TEMpUC19beta-lactamase from Escherichia coli
J. Biol. Chem.
274
23052-23060
1999
Escherichia coli, Escherichia coli JM83
Manually annotated by BRENDA team
Lin, S.; Thomas, M.; Shlaes, D.M.; Rudin, S.D.; Knox, J.R.; Anderson, V.; Bonomo, R.A.
Kinetic analysis of an inhibitor-resistant variant of the OHIO-1 beta-lactamase, an SHV-family class A enzyme
Biochem. J.
333
395-400
1998
Escherichia coli, Escherichia coli DH5-alpha
Manually annotated by BRENDA team
Viadiu, H.; Osuna, J.; Fink, A.L.; Soberon, X.
A new TEM beta-lactamase double mutant with broadened specificity reveals substrate-dependent functional interactions
J. Biol. Chem.
270
781-787
1995
Escherichia coli, Escherichia coli JM101
Manually annotated by BRENDA team
Brun, T.; Peduzzi, J.; Canica, M.M.; Gerard, P.; Nevot, P.; Barthelemy, M.; Labia, R.
Characterization and amino acid sequence of IRT-4, a novel TEM-type enzyme with a decreased susceptibility to beta-lactamase inhibitors
FEMS Microbiol. Lett.
120
111-118
1994
Escherichia coli, Escherichia coli PEY
Manually annotated by BRENDA team
Ledent, P.; Raquet, X.; Joris, B.; Van Beeumen, J.; Frere, J.M.
A comparative study of beta-lactamases
Biochem. J.
292
439-443
1993
Escherichia coli, Escherichia coli JM105
-
Manually annotated by BRENDA team
Trehan, I.; Beadle, B.M.; Shoichet, B.K.
Inhibition of AmpC beta-lactamase through a destabilizing interaction in the active site
Biochemistry
40
7992-7999
2001
Escherichia coli (P00811), Escherichia coli, Escherichia coli JM109 (P00811)
Manually annotated by BRENDA team
Zhang, Z.; Palzkill, T.
Dissecting the protein-protein interface between beta-lactamase inhibitory protein and class A beta-lactamases
J. Biol. Chem.
279
42860-42866
2004
Bacillus anthracis, Serratia marcescens, Klebsiella pneumoniae (P0AD64), Escherichia coli (P62593)
Manually annotated by BRENDA team
Huang, W.; Beharry, Z.; Zhang, Z.; Palzkill, T.
A broad-spectrum peptide inhibitor of beta-lactamase identified using phage display and peptide arrays
Protein Eng.
16
853-860
2003
Enterobacter cloacae, Bacillus anthracis, Escherichia coli
Manually annotated by BRENDA team
Sun, T.; Nukaga, M.; Mayama, K.; Braswell, E.H.; Knox, J.R.
Comparison of beta-lactamases of classes A and D: 1.5-A crystallographic structure of the class D OXA-1 oxacillinase
Protein Sci.
12
82-91
2003
Escherichia coli
Manually annotated by BRENDA team
Doi, Y.; Wachino, J.; Ishiguro, M.; Kurokawa, H.; Yamane, K.; Shibata, N.; Shibayama, K.; Yokoyama, K.; Kato, H.; Yagi, T.; Arakawa, Y.
Inhibitor-sensitive AmpC beta-lactamase variant produced by an Escherichia coli clinical isolate resistant to oxyiminocephalosporins and cephamycins
Antimicrob. Agents Chemother.
48
2652-2658
2004
Escherichia coli (Q76DI4), Escherichia coli, Escherichia coli HKY28 (Q76DI4), Escherichia coli HKY28
Manually annotated by BRENDA team
Munday, C.J.; Boyd, D.A.; Brenwald, N.; Miller, M.; Andrews, J.M.; Wise, R.; Mulvey, M.R.; Hawkey, P.M.
Molecular and kinetic comparison of the novel extended-spectrum beta-lactamases CTX-M-25 and CTX-M-26
Antimicrob. Agents Chemother.
48
4829-4834
2004
Klebsiella pneumoniae (Q8GD10), Klebsiella pneumoniae, Escherichia coli (Q8KSA6), Escherichia coli
Manually annotated by BRENDA team
Brinas, L.; Moreno, M.A.; Teshager, T.; Saenz, Y.; Porrero, M.C.; Dominguez, L.; Torres, C.
Monitoring and characterization of extended-spectrum beta-lactamases in Escherichia coli strains from healthy and sick animals in Spain in 2003
Antimicrob. Agents Chemother.
49
1262-1264
2005
Escherichia coli
Manually annotated by BRENDA team
Bauvois, C.; Ibuka, A.S.; Celso, A.; Alba, J.; Ishii, Y.; Frere, J.M.; Galleni, M.
Kinetic properties of four plasmid-mediated AmpC beta-lactamases
Antimicrob. Agents Chemother.
49
4240-4246
2005
Escherichia coli
Manually annotated by BRENDA team
Alba, J.; Ishii, Y.; Thomson, K.; Moland, E.S.; Yamaguchi, K.
Kinetics study of KPC-3, a plasmid-encoded class A carbapenem-hydrolyzing beta-lactamase
Antimicrob. Agents Chemother.
49
4760-4762
2005
Escherichia coli
Manually annotated by BRENDA team
Villegas, M.V.; Correa, A.; Perez, F.; Miranda, M.C.; Zuluaga, T.; Quinn, J.P.; Quinn, J.P.
Prevalence and characterization of extended-spectrum beta-lactamases in Klebsiella pneumoniae and Escherichia coli isolates from Colombian hospitals
Diagn. Microbiol. Infect. Dis.
49
217-222
2004
Escherichia coli, Klebsiella pneumoniae
Manually annotated by BRENDA team
Bonnefoy, A.; Dupuis-Hamelin, C.; Steier, V.; Delachaume, C.; Seys, C.; Stachyra, T.; Fairley, M.; Guitton, M.; Lampilas, M.
In vitro activity of AVE1330A, an innovative broad-spectrum non-beta-lactam beta-lactamase inhibitor
J. Antimicrob. Chemother.
54
410-417
2004
Enterobacter cloacae, Escherichia coli, Enterobacter cloacae 293HT6
Manually annotated by BRENDA team
Perumal, S.K.; Pratt, R.F.
Synthesis and evaluation of ketophosph(on)ates as beta-lactamase inhibitors
J. Org. Chem.
71
4778-4785
2006
Enterobacter cloacae, Escherichia coli, Enterobacter cloacae P99
Manually annotated by BRENDA team
Liebana, E.; Gibbs, M.; Clouting, C.; Barker, L.; Clifton-Hadley, F.A.; Pleydell, E.; Abdalhamid, B.; Hanson, N.D.; Martin, L.; Poppe, C.; Davies, R.H.
Characterization of beta-lactamases responsible for resistance to extended-spectrum cephalosporins in Escherichia coli and Salmonella enterica strains from food-producing animals in the United Kingdom
Microb. Drug Resist.
10
1-9
2004
Escherichia coli, Salmonella enterica
Manually annotated by BRENDA team
Kanj, S.S.; Corkill, J.E.; Kanafani, Z.A.; Araj, G.F.; Hart, C.A.; Jaafar, R.; Matar, G.M.
Molecular characterisation of extended-spectrum beta-lactamase-producing Escherichia coli and Klebsiella spp. isolates at a tertiary-care centre in Lebanon
Clin. Microbiol. Infect.
14
501-504
2008
Escherichia coli, Klebsiella sp.
Manually annotated by BRENDA team
Ishii, Y.; Galleni, M.; Ma, L.; Frere, J.-M.; Yamaguchi, K.
Biochemical characterisation of the CTX-M-14 beta-lactamase
Int. J. Antimicrob. Agents
29
159-164
2007
Escherichia coli, Escherichia coli TUM1121
Manually annotated by BRENDA team
Bhattacharjee, A.; Sen, M.R.; Prakash, P.; Anupurba, S.
Role of beta-lactamase inhibitors in enterobacterial isolates producing extended-spectrum beta-lactamases
J. Antimicrob. Chemother.
61
309-314
2008
Escherichia coli, Klebsiella sp., Proteus mirabilis
Manually annotated by BRENDA team
Mammeri, H.; Galleni, M.; Nordmann, P.
Role of the Ser-287-Asn replacement in the hydrolysis spectrum extension of AmpC beta -lactamases in Escherichia coli
Antimicrob. Agents Chemother.
53
323-326
2009
Escherichia coli (P00811), Escherichia coli
Manually annotated by BRENDA team
Leonard, D.A.; Hujer, A.M.; Smith, B.A.; Schneider, K.D.; Bethel, C.R.; Hujer, K.M.; Bonomo, R.A.
The role of OXA-1 beta -lactamase Asp66 in the stabilization of the active-site carbamate group and in substrate turnover
Biochem. J.
410
455-462
2008
Escherichia coli (P13661)
Manually annotated by BRENDA team
Lejeune, A.; Pain, R.H.; Charlier, P.; Frere, J.; Matagne, A.
TEM-1 beta -lactamase folds in a nonhierarchical manner with transient non-native interactions involving the C-terminal region
Biochemistry
47
1186-1193
2008
Escherichia coli, Escherichia coli RB791
Manually annotated by BRENDA team
Adediran, S.A.; Pratt, R.F.
Inhibition of serine beta -lactamases by vanadate-catechol complexes
Biochemistry
47
9467-9474
2008
Escherichia coli, Enterobacter cloacae (P05364), Enterobacter cloacae P99 (P05364)
Manually annotated by BRENDA team
Hu, Z.; Spadafora, L.J.; Hajdin, C.E.; Bennett, B.; Crowder, M.W.
Structure and mechanism of copper- and nickel-substituted analogues of metallo-beta -lactamase L1
Biochemistry
48
2981-2989
2009
Escherichia coli
Manually annotated by BRENDA team
Perumal, S.K.; Adediran, S.A.; Pratt, R.F.
beta -Ketophosphonates as beta -lactamase inhibitors: Intramolecular cooperativity between the hydrophobic subsites of a class D beta -lactamase
Bioorg. Med. Chem.
16
6987-6994
2008
Escherichia coli, Escherichia coli (P13661), Escherichia coli (P62593), Enterobacter cloacae (Q59401), Enterobacter cloacae P99 (Q59401), Enterobacter cloacae P99
Manually annotated by BRENDA team
Wang, Q.; Cheng, J.; Chen, Y.; Ye, Y.; Li, J.; Zhang, X.
Characterization of a novel AmpC-type plasmid-mediated beta -lactamase from an Escherichia coli strain isolated in China
Curr. Microbiol.
57
558-563
2008
Escherichia coli (A3RIY0), Escherichia coli, Escherichia coli E384 (A3RIY0), Escherichia coli E384
Manually annotated by BRENDA team
Perez-Llarena, F.J.; Cartelle, M.; Mallo, S.; Beceiro, A.; Perez, A.; Villanueva, R.; Romero, A.; Bonnet, R.; Bou, G.
Structure-function studies of arginine at position 276 in CTX-M beta -lactamases
J. Antimicrob. Chemother.
61
792-797
2008
Escherichia coli (P28585), Escherichia coli
Manually annotated by BRENDA team
Shimamura, T.; Nitanai, Y.; Uchiyama, T.; Matsuzawa, H.
Improvement of crystal quality by surface mutations of beta-lactamase Toho-1
Acta Crystallogr. Sect. F
65
379-382
2009
Escherichia coli (Q47066)
Manually annotated by BRENDA team
Ganta, S.R.; Perumal, S.; Pagadala, S.R.; Samuelsen, O.; Spencer, J.; Pratt, R.F.; Buynak, J.D.
Approaches to the simultaneous inactivation of metallo- and serine-beta-lactamases
Bioorg. Med. Chem. Lett.
19
1618-1622
2009
Enterobacter cloacae, Escherichia coli
Manually annotated by BRENDA team
Wang, J.; Palzkill, T.; Chow, D.
Structural insight into the kinetics and DELTACp of interactions between TEM-1 beta-lactamase and beta-lactamase inhibitory protein (BLIP)
J. Biol. Chem.
284
595-609
2009
Escherichia coli (P62593)
Manually annotated by BRENDA team
Eidam, O.; Romagnoli, C.; Caselli, E.; Babaoglu, K.; Pohlhaus, D.T.; Karpiak, J.; Bonnet, R.; Shoichet, B.K.; Prati, F.
Design, synthesis, crystal structures, and antimicrobial activity of sulfonamide boronic acids as beta-lactamase inhibitors
J. Med. Chem.
53
7852-7863
2010
Escherichia coli (P00811)
Manually annotated by BRENDA team
Guntas, G.; Kanwar, M.; Ostermeier, M.
Circular permutation in the omega-loop of TEM-1 beta-lactamase results in improved activity and altered substrate specificity
PLoS ONE
7
e35998
2012
Escherichia coli (P62593)
Manually annotated by BRENDA team
Ke, W.; Laurent, A.H.; Armstrong, M.D.; Chen, Y.; Smith, W.E.; Liang, J.; Wright, C.M.; Ostermeier, M.; van den Akker, F.
Structure of an engineered beta-lactamase maltose binding protein fusion protein: insights into heterotropic allosteric regulation
PLoS ONE
7
e39168
2012
Escherichia coli (P62593)
Manually annotated by BRENDA team
Mathieu, V.; Fastrez, J.; Soumillion, P.
Engineering allosteric regulation into the hinge region of a circularly permuted TEM-1 beta-lactamase
Protein Eng. Des. Sel.
23
699-709
2010
Escherichia coli
Manually annotated by BRENDA team
Papp-Wallace, K.M.; Mallo, S.; Bethel, C.R.; Taracila, M.A.; Hujer, A.M.; Fernandez, A.; Gatta, J.A.; Smith, K.M.; Xu, Y.; Page, M.G.; Desarbre, E.; Bou, G.; Bonomo, R.A.
A kinetic analysis of the inhibition of FOX-4 beta-lactamase, a plasmid-mediated AmpC cephalosporinase, by monocyclic beta-lactams and carbapenems
J. Antimicrob. Chemother.
69
682-690
2014
Escherichia coli
Manually annotated by BRENDA team
Makena, A.; Brem, J.; Pfeffer, I.; Geffen, R.E.; Wilkins, S.E.; Tarhonskaya, H.; Flashman, E.; Phee, L.M.; Wareham, D.W.; Schofield, C.J.
Biochemical characterization of New Delhi metallo-beta-lactamase variants reveals differences in protein stability
J. Antimicrob. Chemother.
70
463-469
2015
Escherichia coli (A0A024FRL9), Escherichia coli (A0A0F6N6D4), Escherichia coli (H6WET3), Escherichia coli (H6WZS9), Escherichia coli (I3VKD5), Escherichia coli (J7I0S9), Escherichia coli (M1VE66), Klebsiella pneumoniae (C7C422), Klebsiella pneumoniae (S5ZIP8), Klebsiella pneumoniae (T2A6Y2), Acinetobacter baumannii (F2YZ26)
Manually annotated by BRENDA team
Che, T.; Bethel, C.R.; Pusztai-Carey, M.; Bonomo, R.A.; Carey, P.R.
The different inhibition mechanisms of OXA-1 and OXA-24 beta-lactamases are determined by the stability of active site carboxylated lysine
J. Biol. Chem.
289
6152-6164
2014
Acinetobacter baumannii (J9XTR7), Escherichia coli (P13661)
Manually annotated by BRENDA team
Rezai, M.S.; Salehifar, E.; Rafiei, A.; Langaee, T.; Rafati, M.; Shafahi, K.; Eslami, G.
Characterization of multidrug resistant extended-spectrum beta-lactamase-producing Escherichia coli among uropathogens of pediatrics in north of Iran
BioMed Res. Int.
2015
309478
2015
Escherichia coli
Manually annotated by BRENDA team
Koga, V.L.; Maluta, R.P.; da Silveira, W.D.; Ribeiro, R.A.; Hungria, M.; Vespero, E.C.; Nakazato, G.; Kobayashi, R.K.T.
Characterization of CMY-2-type beta-lactamase-producing Escherichia coli isolated from chicken carcasses and human infection in a city of South Brazil
BMC Microbiol.
19
174
2019
Escherichia coli (Q53TY8), Escherichia coli
Manually annotated by BRENDA team
Avci, F.G.; Altinisik, F.E.; Vardar Ulu, D.; Ozkirimli Olmez, E.; Sariyar Akbulut, B.
An evolutionarily conserved allosteric site modulates beta-lactamase activity
J. Enzyme Inhib. Med. Chem.
31
33-40
2016
Escherichia coli (Q6SJ61)
Manually annotated by BRENDA team
Li, S.; Zhu, Z.C.; Wang, L.; Zhou, Y.F.; Tang, Y.J.; Miao, Z.M.
Prevalence and characterization of extended-spectrum beta-lactamase-producing Enterobacteriaceae in spring waters
Lett. Appl. Microbiol.
61
544-548
2015
Klebsiella pneumoniae (D2D9A0), Klebsiella pneumoniae (Q2PUH3), Klebsiella pneumoniae, Escherichia coli (Q0GA57), Escherichia coli (Q840M4), Escherichia coli (Q9EXV5), Escherichia coli (Q9L5C7), Escherichia coli
Manually annotated by BRENDA team
Banerjee, A.; Bardhan, R.; Chowdhury, M.; Joardar, S.N.; Isore, D.P.; Batabyal, K.; Dey, S.; Sar, T.K.; Bandyopadhyay, S.; Dutta, T.K.; Samanta, I.
Characterization of beta-lactamase and biofilm producing Enterobacteriaceae isolated from organized and backyard farm ducks
Lett. Appl. Microbiol.
69
110-115
2019
Escherichia coli, Klebsiella pneumoniae, Salmonella sp.
Manually annotated by BRENDA team
Lee, D.; Das, S.; Dawson, N.L.; Dobrijevic, D.; Ward, J.; Orengo, C.
Novel computational protocols for functionally classifying and characterising serine beta-lactamases
PLoS Comput. Biol.
12
e1004926
2016
Escherichia coli (P62593), Escherichia coli (Q47066)
Manually annotated by BRENDA team