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3-([3-dibenzylamino-3-oxopropanoyl]oxy)benzoic acid + H2O
?
-
-
-
?
3-([3-[benzyl(methyl)amino]-3-oxopropanoyl]oxy)benzoic acid + H2O
?
-
-
-
?
3-([[(2R)-3-(benzylamino)-2-methoxy-3-oxopropanoyl]oxy]methyl)benzoic acid + H2O
?
-
-
-
?
3-([[(2R)-3-(benzylamino)-2-methyl-3-oxopropanoyl]oxy]methyl)benzoic acid + H2O
?
-
-
-
?
3-([[(2S)-3-(benzylamino)-2-methoxy-3-oxopropanoyl]oxy]methyl)benzoic acid + H2O
?
-
-
-
?
3-([[(2S)-3-(benzylamino)-2-methyl-3-oxopropanoyl]oxy]methyl)benzoic acid + H2O
?
-
-
-
?
3-([[2-benzyl-3-oxo-3-(benzylamino)propanoyl]oxy]methyl)benzoic acid + H2O
?
-
-
-
?
3-nitrophenyl (2S)-2-hydroxy-3-phenylpropanoate + H2O
?
-
-
-
?
3-[[(2S)-2-hydroxy-3-phenylpropanoyl]oxy]benzoic acid + H2O
?
-
-
-
?
ampicillin + H2O
(2R,4S)-2-[(R)-[[(2R)-2-amino-2-phenylacetyl]amino](carboxy)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
?
benzyl [[(2R)-2-hydroxy-3-phenylpropanoyl]oxy]carbamate + H2O
? + hydroxamate
-
-
-
?
benzyl [[(2S)-2-hydroxy-2-phenylacetyl]oxy]carbamate + H2O
? + hydroxamate
-
-
-
?
benzyl [[(2S)-2-hydroxy-3-phenylpropanoyl]oxy]carbamate + H2O
? + hydroxamate
-
-
-
?
benzyl [[(2S)-2-hydroxy-4-phenylbutanoyl]oxy]carbamate + H2O
? + hydroxamate
-
-
-
?
benzyl [[(2S)-2-hydroxypropanoyl]oxy]carbamate + H2O
? + hydroxamate
-
-
-
?
benzylpenicillin + H2O
(2R,4S)-2-[(R)-carboxy(2-phenylacetamido)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
?
carbenicillin + H2O
(2R,4S)-2-{(R)-carboxy[2-carboxy(phenyl)acetamido]methyl}-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
?
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
-
-
-
?
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
-
-
-
?
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
-
-
-
?
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
-
-
-
?
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
-
-
-
?
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
-
-
-
?
(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
-
-
-
-
?
(6R,7R)-3-[(acetyloxy)methyl]-7-(hydroxyamino)-8-oxo-5-thia-1-azabicyclo[4.2.0]oct-2-ene-2-carboxylate + H2O
(2R)-5-[(acetyloxy)methyl]-2-[(R)-carboxy(hydroxyamino)methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylate
-
-
-
-
?
(6R,7R)-3-[(acetyloxy)methyl]-7-amino-8-oxo-5-thia-1-azabicyclo[4.2.0]oct-2-ene-2-carboxylate + H2O
(2R)-5-[(acetyloxy)methyl]-2-[(R)-amino(carboxy)methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylate
-
-
-
-
?
(6R,7R)-3-[(acetyloxy)methyl]-7-[formyl(hydroxy)amino]-8-oxo-5-thia-1-azabicyclo[4.2.0]oct-2-ene-2-carboxylate + H2O
(2R)-5-[(acetyloxy)methyl]-2-[(R)-carboxy[formyl(hydroxy)amino]methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylate
-
-
-
-
?
(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
-
-
-
-
?
(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
-
-
-
-
?
(6R,7Z)-3-[(acetyloxy)methyl]-7-(hydroxyimino)-8-oxo-5-thia-1-azabicyclo[4.2.0]oct-2-ene-2-carboxylate + H2O
(2R)-5-[(acetyloxy)methyl]-2-[(Z)-carboxy(hydroxyimino)methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylate
-
-
-
-
?
(6R,7Z)-7-(hydroxyimino)-3-methyl-8-oxo-5-thia-1-azabicyclo[4.2.0]oct-2-ene-2-carboxylate 5,5-dioxide + H2O
(2R)-2-[(Z)-carboxy(hydroxyimino)methyl]-5-methyl-3,6-dihydro-2H-1,3-thiazine-4-carboxylate 1,1-dioxide
-
-
-
-
?
(7R)-7-(benzyloxycarbonylamino)-3-methyl-8-oxo-5-thia-1-azabicyclo[4.2.0]oct-2-ene-2-carboxylate + H2O
2-[(R)-{[(benzyloxy)carbonyl]amino}(carboxy)methyl]-5-methyl-3,6-dihydro-2H-1,3-thiazine-4-carboxylate
-
-
-
-
?
(7S)-7-(benzyloxycarbonylamino)-3-methyl-8-thioxo-5-thia-1-azabicyclo[4.2.0]oct-2-ene-2-carboxylate + H2O
2-[(S)-{[(benzyloxy)carbonyl]amino}(carboxy)methyl]-5-methyl-3,6-dihydro-2H-1,3-thiazine-4-carboxylate
-
is 1000000times poorer (kcat and kcat/Km) as a substrate than (7R)-7-(benzyloxycarbonylamino)-3-methyl-8-oxo-5-thia-1-azabicyclo[4.2.0]oct-2-ene-2-carboxylate
-
-
?
2-(2-(2-phenylacetamido)acetoxy)acetate + H2O
?
-
-
-
-
?
2-(2-(2-phenylacetamido)ethanethioyloxy)acetate + H2O
?
-
2-(2-(2-phenylacetamido)ethanethioyloxy)acetate is much poorer a substrate than 2-(2-(2-phenylacetamido)acetoxy)acetate
-
-
?
3-(2-(2-phenylacetamido)acetoxy)benzoate + H2O
?
-
-
-
-
?
3-([N-(phenylacetyl)glycyl]oxy)benzoic acid + H2O
?
-
-
-
-
?
3-([N-[(2Z)-2-(2-amino-1,3-thiazol-4-yl)-2-(methoxyimino)acetyl]glycyl]oxy)benzoic acid + H2O
?
3-[2-(2-aminothiazol-4-yl)2-(Z)-methoxyiminoacetylglycyl]oxybenzoic acid + H2O
?
-
-
-
-
?
4beta-methoxy-trinem + H2O
(1R,4R,7aS)-1-[(2R)-1-carboxy-2-hydroxypropyl]-4-methoxy-2,4,5,6,7,7a-hexahydro-1H-isoindole-3-carboxylic acid
-
-
-
-
?
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
-
chromophoric substrate
-
-
?
7alpha-aminocephalosporanic acid + H2O
(2R)-5-[(acetyloxy)methyl]-2-[(S)-amino(carboxy)methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
?
7beta-aminocephalosporanic acid + H2O
(2R)-5-[(acetyloxy)methyl]-2-[(R)-amino(carboxy)methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
a beta-lactam + H2O
a substituted beta-amino acid
-
-
-
-
?
a penicillin + H2O
a penicilloic acid
-
-
-
?
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
-
-
-
-
?
ampicillin + H2O
(2R,4S)-2-[(R)-[[(2R)-2-amino-2-phenylacetyl]amino](carboxy)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
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
-
-
-
-
?
aztreonam + H2O
[(1S,2S)-1-[[(2Z)-2-(2-azaniumyl-1,3-thiazol-4-yl)-2- [[(2-carboxypropan-2-yl)oxy]imino]acetyl]amino]-1-carboxypropan-2-yl]sulfamate
-
-
-
?
benzylpenicillin + H2O
(2R,4S)-2-[(R)-carboxy(2-phenylacetamido)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
-
?
cefepime + H2O
(2R)-2-[(R)-[[(2Z)-2-(2-amino-1,3-thiazol-4-yl)-2-(methoxyimino)acetyl]amino](carboxy)methyl]-5-[(1-methylpyrrolidin-1-ium-1-yl)methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylate
-
-
-
?
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
-
-
-
?
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
cefotetan + H2O
(2R)-2-[(S)-{[4-(2-amino-1-carboxy-2-oxoethylidene)-1,3-dithietane-2-carbonyl]amino}(carboxy)methoxymethyl]-5-{[(1-methyl-1H-tetrazol-5-yl)sulfanyl]methyl}-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
-
?
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
-
-
-
-
?
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
-
-
-
?
ceftaxidime + 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
-
-
-
?
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
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
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
-
-
-
-
?
cephaloridine + H2O
(2R)-2-[(R)-carboxy[(thiophen-2-ylacetyl)amino]methyl]-5-(pyridinium-1-ylmethyl)-3,6-dihydro-2H-1,3-thiazine-4-carboxylate
-
-
-
-
?
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
-
-
-
-
?
cephalothin + H2O
(2R)-5-[(acetyloxy)methyl]-2-[(R)-carboxy[(thiophen-2-ylacetyl)amino]methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
imipenem + H2O
(5R)-5-[(1S,2R)-1-carboxy-2-hydroxypropyl]-3-({2-[(iminomethyl)amino]ethyl}sulfanyl)-4,5-dihydro-1H-pyrrole-2-carboxylic acid
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
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
-
-
-
-
?
N-(phenylacetyl)thioglycylglycolic acid + H2O
phenylacetylglycine + glycolate
-
-
-
-
?
penicillin + H2O
?
-
-
-
?
penicillin G + H2O
(2R,4S)-2-[(R)-carboxy[(phenylacetyl)amino]methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
-
?
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
-
-
-
?
sanfetrinem + H2O
(1R,4S,7aS)-1-[(1S,2R)-1-carboxy-2-hydroxypropyl]-4-methoxy-2,4,5,6,7,7a-hexahydro-1H-isoindole-3-carboxylic acid
-
-
-
-
?
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
-
-
-
-
?
additional information
?
-
3-([N-[(2Z)-2-(2-amino-1,3-thiazol-4-yl)-2-(methoxyimino)acetyl]glycyl]oxy)benzoic acid + H2O
?
-
GC1 beta-lactamase
-
-
?
3-([N-[(2Z)-2-(2-amino-1,3-thiazol-4-yl)-2-(methoxyimino)acetyl]glycyl]oxy)benzoic acid + H2O
?
-
P99 beta-lactamase
-
-
?
7beta-aminocephalosporanic acid + H2O
(2R)-5-[(acetyloxy)methyl]-2-[(R)-amino(carboxy)methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
-
?
7beta-aminocephalosporanic acid + H2O
(2R)-5-[(acetyloxy)methyl]-2-[(R)-amino(carboxy)methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
?
ampicillin + H2O
(2R,4S)-2-[(R)-[[(2R)-2-amino-2-phenylacetyl]amino](carboxy)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
?
ampicillin + H2O
(2R,4S)-2-[(R)-[[(2R)-2-amino-2-phenylacetyl]amino](carboxy)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
?
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
-
-
-
-
?
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
-
-
-
?
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
-
-
-
?
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
-
conformational restriction of the extended OMEGA loop in the enzyme is probably responsible for the long-living acyl-enzyme intermediate and transition effects of cefotaxime
-
-
?
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
-
GC1 beta-lactamase
-
-
?
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
-
poor substrate for P99 beta-lactamase
-
-
?
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
-
-
-
-
?
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
-
-
-
?
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
-
cephalosporin antibiotic
-
-
?
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
-
-
-
-
?
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
-
GC1 beta-lactamase
-
-
?
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
-
poor substrate for P99 beta-lactamase
-
-
?
cephalothin + H2O
(2R)-5-[(acetyloxy)methyl]-2-[(R)-carboxy[(thiophen-2-ylacetyl)amino]methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
-
?
cephalothin + H2O
(2R)-5-[(acetyloxy)methyl]-2-[(R)-carboxy[(thiophen-2-ylacetyl)amino]methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
best substrate
-
-
?
cephalothin + H2O
(2R)-5-[(acetyloxy)methyl]-2-[(R)-carboxy[(thiophen-2-ylacetyl)amino]methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
GC1 beta-lactamase
-
-
?
cephalothin + H2O
(2R)-5-[(acetyloxy)methyl]-2-[(R)-carboxy[(thiophen-2-ylacetyl)amino]methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
P99 beta-lactamase
-
-
?
imipenem + H2O
(5R)-5-[(1S,2R)-1-carboxy-2-hydroxypropyl]-3-({2-[(iminomethyl)amino]ethyl}sulfanyl)-4,5-dihydro-1H-pyrrole-2-carboxylic acid
-
-
-
-
?
imipenem + H2O
(5R)-5-[(1S,2R)-1-carboxy-2-hydroxypropyl]-3-({2-[(iminomethyl)amino]ethyl}sulfanyl)-4,5-dihydro-1H-pyrrole-2-carboxylic acid
-
-
-
?
imipenem + H2O
(5R)-5-[(1S,2R)-1-carboxy-2-hydroxypropyl]-3-({2-[(iminomethyl)amino]ethyl}sulfanyl)-4,5-dihydro-1H-pyrrole-2-carboxylic acid
-
beta-lactam antibiotic
-
-
?
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
-
-
-
-
?
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
-
-
-
?
additional information
?
-
O-(1-carboxy-1-alkyloxycarbonyl) hydroxamates are found to spontaneously decarboxylate in aqueous neutral buffer to form O-(2-hydroxyalkylcarbonyl) hydroxamates.While the former molecules do not react rapidly with serine beta-lactamases, the latter are quite good substrates of representative class A and C, but not D enzymes. The enzymes catalyze hydrolysis of these compounds to a mixture of the R-hydroxy acid and hydroxamate. Although both D- and L-R-hydroxy acid derivatives were substrates, the former are preferred
-
-
?
additional information
?
-
substituted aryl malonamates are substrates of class A and class C beta-lactamases, and of soluble DD-peptidases
-
-
?
additional information
?
-
-
cephalosporins bearing oximino side chains are resistant to hydrolysis by class C enzymes, the side chain is necessary but not sufficent for production of resistance, it must be combinated with the dihydrothiazine ring
-
-
?
additional information
?
-
-
no activity with the thiono analogue of N-(phenylacetyl)thioglycylglycolic acid
-
-
?
additional information
?
-
-
3-(2-(N-methyl-2-phenylacetamido)acetoxy)benzoate is not a substrate
-
-
?
additional information
?
-
substrate specificity in vivo, overview
-
-
-
additional information
?
-
substrate specificity in vivo, overview
-
-
-
additional information
?
-
substrate specificity in vivo, overview
-
-
-
additional information
?
-
substrate specificity in vivo, overview
-
-
-
additional information
?
-
substrate specificity in vivo, overview
-
-
-
additional information
?
-
substrate specificity in vivo, overview
-
-
-
additional information
?
-
substrate specificity in vivo, overview
-
-
-
additional information
?
-
-
substrate specificity in vivo, overview
-
-
-
additional information
?
-
substrate specificity in vivo, overview. Aztreonam and cefepime are poor substrates
-
-
-
additional information
?
-
substrate specificity in vivo, overview. Aztreonam and cefepime are poor substrates
-
-
-
additional information
?
-
substrate specificity in vivo, overview. Aztreonam and cefepime are poor substrates
-
-
-
additional information
?
-
substrate specificity in vivo, overview. Aztreonam and cefepime are poor substrates
-
-
-
additional information
?
-
substrate specificity in vivo, overview. Aztreonam and cefepime are poor substrates
-
-
-
additional information
?
-
substrate specificity in vivo, overview. Aztreonam and cefepime are poor substrates
-
-
-
additional information
?
-
substrate specificity in vivo, overview. Aztreonam and cefepime are poor substrates
-
-
-
additional information
?
-
-
substrate specificity in vivo, overview. Aztreonam and cefepime are poor substrates
-
-
-
additional information
?
-
substrate specificity in vivo, overview. Cefotaxime and cefepime are poor substrates
-
-
-
additional information
?
-
substrate specificity in vivo, overview. Cefotaxime and cefepime are poor substrates
-
-
-
additional information
?
-
substrate specificity in vivo, overview. Cefotaxime and cefepime are poor substrates
-
-
-
additional information
?
-
substrate specificity in vivo, overview. Cefotaxime and cefepime are poor substrates
-
-
-
additional information
?
-
substrate specificity in vivo, overview. Cefotaxime and cefepime are poor substrates
-
-
-
additional information
?
-
substrate specificity in vivo, overview. Cefotaxime and cefepime are poor substrates
-
-
-
additional information
?
-
substrate specificity in vivo, overview. Cefotaxime and cefepime are poor substrates
-
-
-
additional information
?
-
-
substrate specificity in vivo, overview. Cefotaxime and cefepime are poor substrates
-
-
-
additional information
?
-
substrate specificity in vivo, overview. Cefotaxime is a poor enzyme
-
-
-
additional information
?
-
substrate specificity in vivo, overview. Cefotaxime is a poor enzyme
-
-
-
additional information
?
-
substrate specificity in vivo, overview. Cefotaxime is a poor enzyme
-
-
-
additional information
?
-
substrate specificity in vivo, overview. Cefotaxime is a poor enzyme
-
-
-
additional information
?
-
substrate specificity in vivo, overview. Cefotaxime is a poor enzyme
-
-
-
additional information
?
-
substrate specificity in vivo, overview. Cefotaxime is a poor enzyme
-
-
-
additional information
?
-
substrate specificity in vivo, overview. Cefotaxime is a poor enzyme
-
-
-
additional information
?
-
-
substrate specificity in vivo, overview. Cefotaxime is a poor enzyme
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
a beta-lactam + H2O
a substituted beta-amino acid
-
-
-
-
?
ampicillin + H2O
(2R,4S)-2-[(R)-[[(2R)-2-amino-2-phenylacetyl]amino](carboxy)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
-
-
?
aztreonam + H2O
[(1S,2S)-1-[[(2Z)-2-(2-azaniumyl-1,3-thiazol-4-yl)-2- [[(2-carboxypropan-2-yl)oxy]imino]acetyl]amino]-1-carboxypropan-2-yl]sulfamate
-
-
-
?
cefepime + H2O
(2R)-2-[(R)-[[(2Z)-2-(2-amino-1,3-thiazol-4-yl)-2-(methoxyimino)acetyl]amino](carboxy)methyl]-5-[(1-methylpyrrolidin-1-ium-1-yl)methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylate
-
-
-
?
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
-
-
-
?
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
-
-
-
?
ceftaxidime + 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
-
-
-
?
additional information
?
-
additional information
?
-
-
cephalosporins bearing oximino side chains are resistant to hydrolysis by class C enzymes, the side chain is necessary but not sufficent for production of resistance, it must be combinated with the dihydrothiazine ring
-
-
?
additional information
?
-
substrate specificity in vivo, overview
-
-
-
additional information
?
-
substrate specificity in vivo, overview
-
-
-
additional information
?
-
substrate specificity in vivo, overview
-
-
-
additional information
?
-
substrate specificity in vivo, overview
-
-
-
additional information
?
-
substrate specificity in vivo, overview
-
-
-
additional information
?
-
substrate specificity in vivo, overview
-
-
-
additional information
?
-
substrate specificity in vivo, overview
-
-
-
additional information
?
-
-
substrate specificity in vivo, overview
-
-
-
additional information
?
-
substrate specificity in vivo, overview. Aztreonam and cefepime are poor substrates
-
-
-
additional information
?
-
substrate specificity in vivo, overview. Aztreonam and cefepime are poor substrates
-
-
-
additional information
?
-
substrate specificity in vivo, overview. Aztreonam and cefepime are poor substrates
-
-
-
additional information
?
-
substrate specificity in vivo, overview. Aztreonam and cefepime are poor substrates
-
-
-
additional information
?
-
substrate specificity in vivo, overview. Aztreonam and cefepime are poor substrates
-
-
-
additional information
?
-
substrate specificity in vivo, overview. Aztreonam and cefepime are poor substrates
-
-
-
additional information
?
-
substrate specificity in vivo, overview. Aztreonam and cefepime are poor substrates
-
-
-
additional information
?
-
-
substrate specificity in vivo, overview. Aztreonam and cefepime are poor substrates
-
-
-
additional information
?
-
substrate specificity in vivo, overview. Cefotaxime and cefepime are poor substrates
-
-
-
additional information
?
-
substrate specificity in vivo, overview. Cefotaxime and cefepime are poor substrates
-
-
-
additional information
?
-
substrate specificity in vivo, overview. Cefotaxime and cefepime are poor substrates
-
-
-
additional information
?
-
substrate specificity in vivo, overview. Cefotaxime and cefepime are poor substrates
-
-
-
additional information
?
-
substrate specificity in vivo, overview. Cefotaxime and cefepime are poor substrates
-
-
-
additional information
?
-
substrate specificity in vivo, overview. Cefotaxime and cefepime are poor substrates
-
-
-
additional information
?
-
substrate specificity in vivo, overview. Cefotaxime and cefepime are poor substrates
-
-
-
additional information
?
-
-
substrate specificity in vivo, overview. Cefotaxime and cefepime are poor substrates
-
-
-
additional information
?
-
substrate specificity in vivo, overview. Cefotaxime is a poor enzyme
-
-
-
additional information
?
-
substrate specificity in vivo, overview. Cefotaxime is a poor enzyme
-
-
-
additional information
?
-
substrate specificity in vivo, overview. Cefotaxime is a poor enzyme
-
-
-
additional information
?
-
substrate specificity in vivo, overview. Cefotaxime is a poor enzyme
-
-
-
additional information
?
-
substrate specificity in vivo, overview. Cefotaxime is a poor enzyme
-
-
-
additional information
?
-
substrate specificity in vivo, overview. Cefotaxime is a poor enzyme
-
-
-
additional information
?
-
substrate specificity in vivo, overview. Cefotaxime is a poor enzyme
-
-
-
additional information
?
-
-
substrate specificity in vivo, overview. Cefotaxime is a poor enzyme
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
N-hydroxybenzenesulfonamide
weak inhibition
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-hydroxybenzohydroxamic acid complex
-
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-methoxybenzohydroxamic acid complex
-
-
vanadate/4-nitrobenzene-1,2-diol complex
competitive inhibition, 1:1 complexes of vanadate with a variety of catechols
vanadate/4-nitrobenzohydroxamic acid complex
-
-
vanadate/benzohydroxamic acid complex
-
vanadate/benzylhydroxamic acid complex
-
vanadate/biphenyl-3,4-diol complex
competitive inhibition, 1:1 complexes of vanadate with a variety of catechols
vanadate/cyclohexene-1-hydroxamic acid complex
-
vanadate/hydroxamic acid complexes
competitive inhibition mechanism, low concentrations of 1:1 complexes of vanadate with hydroxamic acids, the hydroxamic acid functional group is essential for inhibition, complex structure, overview, complex modeling
-
vanadate/methylhydroxamic acid complex
-
-
vanadate/N-methylbenzohydroxamic acid complex
-
-
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
(R)-3-(N-benzyloxycarbonylamino)-2-oxo-butylphosphate
-
-
(RS)-4-(N-benzyloxycarbonyl)amino-3-oxo-2-butylphosphate
-
-
3-((benzyloxycarbonylaminooxy)carbonyloxy)benzoic acid
-
o-aryloxycarbonyl hydroxamate, cephalothin as substrate, competitive inhibition, inhibits irreversibly
3-(N-benzyloxycarbonyl)amino-2-oxopropylphenylphosphonate
-
-
3-(N-benzyloxycarbonyl)amino-2-oxopropylphosphate
-
-
3-(N-benzyloxycarbonyl)amino-2-oxopropylphosphonate
-
-
3-[[([[(phenylacetyl)oxy]amino]oxy)carbonyl]oxy]benzoate
-
5 mM
4-(N-benzyloxycarbonyl)amino-3-oxobutylphosphonate
-
-
AAGHYY
-
synthetic peptide, derived from screenings using phage display and peptide arrays
benzyl (4-chlorophenoxy)carbonyloxycarbamate
-
o-aryloxycarbonyl hydroxamate, cephalothin as substrate, competitive inhibition, inhibits irreversibly
benzyl (4-methoxyphenoxy)carbonyloxycarbamate
-
o-aryloxycarbonyl hydroxamate, cephalothin as substrate, competitive inhibition, inhibits irreversibly
benzyl (4-nitrophenoxy)carbonyloxycarbamate
-
o-aryloxycarbonyl hydroxamate, cephalothin as substrate, competitive inhibition, inhibits irreversibly
benzyl (naphthalen-2-yloxy)carbonyloxycarbamate
-
o-aryloxycarbonyl hydroxamate, cephalothin as substrate, competitive inhibition, inhibits irreversibly
benzyl carbonylbis(oxy)dicarbamate
-
o-aryloxycarbonyl hydroxamate, cephalothin as substrate, competitive inhibition, inhibits irreversibly
benzyl methoxycarbonyloxycarbamate
-
o-aryloxycarbonyl hydroxamate, cephalothin as substrate, competitive inhibition, inhibits irreversibly
benzyl methyl(phenoxycarbonyloxy)carbamate
-
o-aryloxycarbonyl hydroxamate, cephalothin as substrate, competitive inhibition, inhibits slightly, 20fold less effectiv than benzyl phenoxycarbonyloxycarbamate
benzyl phenoxycarbonothioyloxycarbamate
-
o-aryloxycarbonyl hydroxamate, cephalothin as substrate, competitive inhibition, inhibits slightly
benzyl phenoxycarbonyloxycarbamate
-
o-aryloxycarbonyl hydroxamate, cephalothin as substrate, competitive inhibition, inhibits irreversibly
benzyl phenylcarbamoyloxycarbamate
-
o-aryloxycarbonyl hydroxamate, cephalothin as substrate, competitive inhibition, inhibits irreversibly
biphenyl-4-ylmethyl phenoxycarbonyloxycarbamate
-
completely inactivated, 2 micro M concentration, o-aryloxycarbonyl hydroxamate, cephalothin as substrate, competitive inhibition, inhibits irreversibly
brobactam
-
best inhibitory effect
cefuroxime
-
competitive inhibition of cephalothin hydrolysis
EDTA
0.02 mM, 50% inhibition
ethyl 3-(benzyloxycarbonyl)amino-2-oxo-1,1-difluoropropylphosphonate
-
-
HSAYSDTRRGDYG
-
synthetic peptide, derived from screenings using phage display and peptide arrays
methyl 3-(N-benzyloxycarbonyl)amino-2-oxo-1-propylphosphate
-
-
N-(phenoxycarbonyloxy)benzenesulfonamide
-
o-aryloxycarbonyl hydroxamate, cephalothin as substrate, competitive inhibition, inhibits irreversibly
N-(phenylacetyl)thioglycylglycolic acid
-
weak reversible inhibition
N-[N'-(benzyloxycarbonyl)aminoacetyl]amino-methylphosphonate
-
-
phenyl 3-(N-benzyloxycarbonyl)amino-2-oxopropylphosphate
-
-
phenyl 3-(N-benzyloxycarbonyl)amino-2-oxopropylphosphonate
-
-
RRGHYY
-
synthetic peptide, derived from screenings using phage display and peptide arrays, inhibition mechanism
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
-
thiono derivative of N-(phenylacetyl)thioglycylglycolic acid
-
weak reversible inhibition
-
[(phenoxycarbonyl)oxy][(phenylacetyl)oxy]amine
-
0.01 mM, irreversible inhibition
cefotaxime
-
competitive inhibition of cephalothin hydrolysis
cefotaxime
-
inhibits hydrolysis of cephalothin, P99 beta-lactamase
clavulanic acid
-
-
clavulanic acid
-
IC50: 1 mM
tazobactam
-
-
tazobactam
-
IC50: 5000 nM
additional information
inhibition kinetics
-
additional information
inhibition by vanadate-catechol complex. 0.1 mM vanadate, varied catechol
-
additional information
vanadate alone (to 1.0 mM) and catechol alone (to 2.0 mM) do not inhibit. Compounds that afford no inhibition are 2,3-dihydroxybenzoic acid, 2,3-dihydroxypyridine (3-hydroxypyrid-2-one), cis-1,2-dihydroxycyclohexane, and L-mandelic acid
-
additional information
-
no inhibition by Arg-Arg
-
additional information
beta-ketophosphonates are less effective against OXA-10 enzyme, effective inhibitors of the class D OXA-1 enzyme and the class C P99 enzyme
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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Ross, G.W.
beta-Lactamase (Enterobacter species)
Methods Enzymol.
43
678-687
1975
Enterobacter cloacae, Enterobacter sp., Enterobacter cloacae P99
brenda
Ross, G.W.; Boulton, M.G.
Purification of beta-lactamases on QAE-sephadex
Biochim. Biophys. Acta
309
430-439
1973
Klebsiella aerogenes, Enterobacter cloacae, Enterobacter cloacae P99, Klebsiella aerogenes 1082E
brenda
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
-
brenda
Mariotte-Boyer, S.; Nicolas-Chanoine, M.H.; Labia, R.
A kinetic study of NMC-A beta-lactamase, an Ambler class A carbapenemase also hydrolysing cephamycins
FEMS Microbiol. Lett.
143
29-33
1996
Enterobacter cloacae, Enterobacter cloacae NOR-1
brenda
Bell, J.H.; Pratt, R.F.
Mechanism of inhibition of the beta-lactamase of Enterobacter cloacae P99 by 1:1 complexes of vanadate with hydroxamic acids
Biochemistry
41
4329-4338
2002
Enterobacter cloacae (P05364), Enterobacter cloacae P99 (P05364), Enterobacter cloacae P99
brenda
Kumar, S.; Adediran, S.A.; Nukaga, M.; Pratt, R.F.
Kinetics of turnover of cefotaxime by the Enterobacter cloacae P99 and GCl beta-lactamases: two free enzyme forms of the P99 beta-lactamase detected by a combination of pre- and post-steady state kinetics
Biochemistry
43
2664-2672
2004
Enterobacter cloacae, Enterobacter cloacae P99, Enterobacter cloacae GC1
brenda
Curley, K.; Pratt, R.F.
The oxyanion hole in serine beta-lactamase catalysis: interactions of thiono substrates with the active site
Bioorg. Chem.
28
338-356
2000
Enterobacter cloacae, Enterobacter cloacae P99
brenda
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
brenda
Gacar, G.G.; Midilli, K.; Kolayli, F.; Ergen, K.; Gundes, S.; Hosoglu, S.; Karadenizli, A.; Vahaboglu, H.
Genetic and enzymatic properties of metallo-beta-lactamase VIM-5 from a clinical isolate of Enterobacter cloacae
Antimicrob. Agents Chemother.
49
4400-4403
2005
Enterobacter cloacae (Q4ZE97), Enterobacter cloacae
brenda
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
brenda
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
brenda
Michaux, C.; Massant, J.; Kerff, F.; Frere, J.M.; Docquier, J.D.; Vandenberghe, I.; Samyn, B.; Pierrard, A.; Feller, G.; Charlier, P.; Van Beeumen, J.; Wouters, J.
Crystal structure of a cold-adapted class C beta-lactamase
FEBS J.
275
1687-1697
2008
Psychrobacter immobilis, Serratia marcescens, Enterobacter cloacae (P05364), Pseudomonas fluorescens (P85302), Pseudomonas fluorescens, Pseudomonas fluorescens TAE4 (P85302), Enterobacter cloacae 908R (P05364)
brenda
Wyrembak, P.N.; Babaoglu, K.; Pelto, R.B.; Shoichet, B.K.; Pratt, R.F.
O-aryloxycarbonyl hydroxamates: New beta-lactamase inhibitors that cross-link the active Site
J. Am. Chem. Soc.
129
9548-9549
2007
Enterobacter cloacae, Enterobacter cloacae P99
brenda
Picao, R.C.; Andrade, S.S.; Nicoletti, A.G.; Campana, E.H.; Moraes, G.C.; Mendes, R.E.; Gales, A.C.
Metallo-beta-Lactamase detection: comparative evaluation of double-disk synergy versus combined disk tests for IMP, GIM, SIM, SPM or VIM-producing isolates
J. Clin. Microbiol.
46
2028-2037
2008
Acinetobacter sp., Enterobacter cloacae, Klebsiella pneumoniae, Pseudomonas aeruginosa, Pseudomonas putida, Serratia marcescens
brenda
Pelto, R.B.; Pratt, R.F.
Kinetics and mechanism of inhibition of a serine beta -lactamase by O-aryloxycarbonyl hydroxamates
Biochemistry
47
12037-12046
2008
Enterobacter cloacae, Enterobacter cloacae P99
brenda
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)
brenda
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
brenda
Fenollar-Ferrer, C.; Frau, J.; Donoso, J.; Munoz, F.
Evolution of class C beta -lactamases: factors influencing their hydrolysis and recognition mechanisms
Theor. Chem. Acc.
121
209-218
2008
Enterobacter cloacae, Enterobacter cloacae P99
-
brenda
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
brenda
Pelto, R.B.; Pratt, R.F.
Serendipitous discovery of alpha-hydroxyalkyl esters as beta-lactamase substrates
Biochemistry
49
10496-10506
2010
Enterobacter cloacae (P05364)
brenda
Adediran, S.; Cabaret, D.; Lohier, J.; Wakselman, M.; Pratt, R.
Substituted aryl malonamates as new serine beta-lactamase substrates: structure-activity studies
Bioorg. Med. Chem.
18
282-291
2010
Enterobacter cloacae (P05364)
brenda
Porres-Osante, N.; Saenz, Y.; Somalo, S.; Torres, C.
Characterization of beta-lactamases in faecal Enterobacteriaceae recovered from healthy humans in Spain focusing on AmpC polymorphisms
Microb. Ecol.
70
132-140
2015
Citrobacter freundii (A3RLA9), Citrobacter freundii (H6UZZ2), Citrobacter freundii (H6UZZ8), Citrobacter freundii (I3QHT4), Citrobacter freundii (I3QHT7), Citrobacter freundii (X2EXH4), Citrobacter freundii, Citrobacter braakii (K0GES5), Citrobacter braakii (K0GET7), Citrobacter braakii (K0GG60), Citrobacter braakii, Enterobacter cloacae (K0GEV1), Enterobacter cloacae (K0GEV3), Enterobacter cloacae (K0GG70), Enterobacter cloacae (Q8KP20), Enterobacter cloacae (X2EXI0), Enterobacter cloacae (X2EXI1), Enterobacter cloacae (X2EXI6), Enterobacter cloacae
brenda