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Information on EC 3.5.2.6 - beta-lactamase and Organism(s) Stenotrophomonas maltophilia and UniProt Accession Q9RBQ1

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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.
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This record set is specific for:
Stenotrophomonas maltophilia
UNIPROT: Q9RBQ1
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Word Map
The taxonomic range for the selected organisms is: Stenotrophomonas maltophilia
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
Beta lactamase OXA-10
-
-
-
-
beta-lactamase
-
-
-
-
beta-lactamase AME I
-
-
-
-
beta-lactamase II
-
-
-
-
BLAIMP
-
-
-
-
carbapenemase
-
-
-
-
Carbenicillinase
-
-
-
-
cefotaximase
-
-
-
-
ceftazidimase
-
-
-
-
cefurooximase
-
-
-
-
Cefuroximase
-
-
-
-
Cephalosporinase
-
-
-
-
class B metallo-beta-lactamase L-1
-
-
Imipenem-cefoxitin hydrolyzing enzyme
-
-
-
-
imipenemase
-
-
-
-
L1 metallo-beta-lactamase
-
metallo-beta-lactamase
-
-
-
-
metallo-beta-lactamase L1
-
neutrapen
-
-
-
-
New Delhi metallo-beta-lactamase-1
-
Oxacillinase
-
-
-
-
penicillinase
-
-
-
-
SHV-2A
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
a beta-lactam + H2O = a substituted beta-amino acid
show the reaction diagram
active site, Asp120 is important for catalysis, as well as substrate and Zn2+ binding
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
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
azlocillin + H2O
(2R,4S)-2-[(R)-carboxy({(2R)-2-[(2-oxoimidazolidine-1-carbonyl)amino]-2-phenylacetyl}amino)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
show the reaction diagram
-
-
-
-
?
biapenem + H2O
(4R,5S)-5-[(1S,2R)-1-carboxy-2-hydroxypropyl]-3-[(6,7-dihydro-5H-pyrazolo[1,2-a][1,2,4]triazol-4-ium-6-yl)sulfanyl]-4-methyl-4,5-dihydro-1H-pyrrole-2-carboxylate
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
cefadroxil + H2O
(2R)-2-[(R)-{[(2R)-2-amino-2-(4-hydroxyphenyl)acetyl]amino}(carboxy)methyl]-5-methyl-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
show the reaction diagram
-
-
-
-
?
cefazolin + H2O
(2R)-2-[(R)-carboxy[2-(1H-tetrazol-1-yl)acetamido]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
-
-
-
?
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
-
-
-
-
?
cefmetazole + H2O
(2R)-2-[(S)-carboxy{2-[(cyanomethyl)sulfanyl]acetamido}methoxymethyl]-5-{[(1-methyl-1H-tetrazol-5-yl)sulfanyl]methyl}-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
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
cefprozil + H2O
(2R)-2-[(R)-{[(2R)-2-amino-2-(4-hydroxyphenyl)acetyl]amino}(carboxy)methyl]-5-[(1E)-prop-1-en-1-yl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
show the reaction diagram
-
-
-
-
?
cefsulodin + H2O
(2R)-5-[(4-carbamoylpyridin-1-ium-1-yl)methyl]-2-[(R)-carboxy{[(2R)-2-phenyl-2-sulfoacetyl]amino}methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylate
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
-
-
-
-
?
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
-
-
-
-
?
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 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
-
-
-
?
cephradine + H2O
(2R)-2-[(R)-{[(2R)-2-amino-2-(cyclohexa-1,4-dien-1-yl)acetyl]amino}(carboxy)methyl]-5-methyl-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
show the reaction diagram
-
-
-
-
?
clavulanic acid + H2O
(2R,4R,5Z)-2-(carboxymethyl)-5-(2-hydroxyethylidene)-1,3-oxazolidine-4-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
-
-
-
?
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
penicillin G + H2O
(2R,4S)-2-[(R)-carboxy[(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
-
-
-
-
?
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
-
-
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Co2+
mononuclear Co(2+)- and Fe(3+)-containing lactamase L1 are essentially inactive
Fe3+
mononuclear Co(2+)- and Fe(3+)-containing lactamase L1 are essentially inactive
additional information
mononuclear metal ion containing and heterobimetallic analogues of the enzyme are generated and characterized using kinetic and spectroscopic studies. Heterobimetallic analogues (ZnCoL1, ZnFeL1, FeFeL1, and CoCoL1) analogues of L1 are generated, and stopped flow kinetic studies revealed that these enzymes rapidly hydrolyze nitrocefin and that there are large amounts of the reaction intermediate formed during the reaction
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1-(2S)-3-mercapto-2-methyl-propionyl-D-proline
competitive inhibitor
2,5-diphenyl-2H-pyrazol-3,4-dicarboxylic acid
-
2,5-diphenyl-3,4-furan dicarboxylic acid
-
2-(((3-mercapto-5-(2-methylphenyl)-4H-1,2,4-triazol-4-yl)imino)methyl)benzoic acid
most effective inhibitor
2-[[5-(2-hydroxyphenyl)-1,3,4-oxadiazol-2-yl]sulfanyl]-N-phenylacetamide
-
2-[[5-(2-hydroxyphenyl)-1,3,4-thiadiazol-2-yl]sulfanyl]-N-phenylacetamide
-
2-[[5-(2-hydroxyphenyl)-4H-1,2,4-triazol-3-yl]sulfanyl]-N-phenylacetamide
-
bulgecin A
partial non-competitive inhibition
Cys-Val-His-Ser-Pro-Asn-Arg-Glu-Cys
-
mixed inhibition
galangin
-
flavonoid, inhibition is not reversible by addition of Zn2+, orientation in the active site, the 4-keto and the 5-hydroxy groups bind to the Zn1 atom of the enzyme
N-(1,3-benzothiazol-2-yl)-2-[[5-(2-hydroxyphenyl)-1,3,4-oxadiazol-2-yl]sulfanyl]acetamide
-
N-(1,3-benzothiazol-2-yl)-2-[[5-(2-hydroxyphenyl)-1,3,4-thiadiazol-2-yl]sulfanyl]acetamide
-
N-(1,3-benzothiazol-2-yl)-2-[[5-(2-hydroxyphenyl)-4H-1,2,4-triazol-3-yl]sulfanyl]acetamide
-
N-(1,3-benzothiazol-2-yl)-2-[[5-(pyridin-3-yl)-1,3,4-oxadiazol-2-yl]sulfanyl]acetamide
-
N-(1,3-benzothiazol-2-yl)-2-[[5-(pyridin-3-yl)-1,3,4-thiadiazol-2-yl]sulfanyl]acetamide
-
N-(1,3-benzothiazol-2-yl)-2-[[5-(pyridin-3-yl)-4H-1,2,4-triazol-3-yl]sulfanyl]acetamide
-
N-(1,3-benzothiazol-2-yl)-2-[[5-(pyridin-4-yl)-1,3,4-oxadiazol-2-yl]sulfanyl]acetamide
-
N-(1,3-benzothiazol-2-yl)-2-[[5-(pyridin-4-yl)-1,3,4-thiadiazol-2-yl]sulfanyl]acetamide
-
N-(1,3-benzothiazol-2-yl)-2-[[5-(pyridin-4-yl)-4H-1,2,4-triazol-3-yl]sulfanyl]acetamide
-
N-phenyl-2-[[5-(pyridin-4-yl)-1,3,4-oxadiazol-2-yl]sulfanyl]acetamide
-
N-phenyl-2-[[5-(pyridin-4-yl)-1,3,4-thiadiazol-2-yl]sulfanyl]acetamide
-
N-phenyl-2-[[5-(pyridin-4-yl)-4H-1,2,4-triazol-3-yl]sulfanyl]acetamide
-
N-[(benzyloxy) carbonyl]-L-cysteinyl glycine
-
quercetin
-
flavonoid
additional information
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.055 - 1.33
ampicillin
0.06
azlocillin
-
-
0.032 - 0.128
biapenem
0.013 - 0.55
cefaclor
0.25
cefadroxil
-
-
0.004
cefmetazole
-
-
0.16
cefotaxime
-
-
0.0011 - 0.098
cefoxitin
0.03
cefsulodin
-
-
0.008
ceftizoxime
-
-
0.13
cefuroxime
-
-
0.17
cephaloridine
-
-
0.18
cephalosporin C
-
-
0.0089 - 0.15
cephalothin
0.26
cephradine
-
-
0.022
clavulanic acid
-
-
0.057 - 0.31
Imipenem
0.015 - 0.097
meropenem
0.005
moxalactam
-
-
0.0023 - 0.103
nitrocefin
0.038 - 0.384
penicillin G
0.2
piperacillin
-
-
0.49
ticarcillin
-
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.01 - 580
ampicillin
0.3 - 134
biapenem
0.28 - 60
cefaclor
4.7
cefmetazole
-
-
0.34 - 2.2
cefoxitin
0.0833
cefsulodin
-
-
2.7
ceftizoxime
-
-
67
cephaloridine
-
-
280
cephalosporin C
-
-
0.31 - 82
cephalothin
11
clavulanic acid
-
-
0.36 - 370
Imipenem
0.29 - 157
meropenem
0.15
moxalactam
-
-
0.028 - 63
nitrocefin
0.01 - 600
penicillin G
420
piperacillin
-
-
440
ticarcillin
-
-
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.00034
2-[[5-(2-hydroxyphenyl)-1,3,4-oxadiazol-2-yl]sulfanyl]-N-phenylacetamide
pH and temperature not specified in the publication
0.00051
2-[[5-(2-hydroxyphenyl)-1,3,4-thiadiazol-2-yl]sulfanyl]-N-phenylacetamide
pH and temperature not specified in the publication
0.000073
2-[[5-(2-hydroxyphenyl)-4H-1,2,4-triazol-3-yl]sulfanyl]-N-phenylacetamide
pH and temperature not specified in the publication
0.0025
bulgecin A
25°C, pH 7.0
0.009 - 0.016
Cys-Val-His-Ser-Pro-Asn-Arg-Glu-Cys
0.00065
N-(1,3-benzothiazol-2-yl)-2-[[5-(2-hydroxyphenyl)-1,3,4-oxadiazol-2-yl]sulfanyl]acetamide
pH and temperature not specified in the publication
0.0018
N-(1,3-benzothiazol-2-yl)-2-[[5-(2-hydroxyphenyl)-1,3,4-thiadiazol-2-yl]sulfanyl]acetamide
pH and temperature not specified in the publication
0.00025
N-(1,3-benzothiazol-2-yl)-2-[[5-(2-hydroxyphenyl)-4H-1,2,4-triazol-3-yl]sulfanyl]acetamide
pH and temperature not specified in the publication
0.001
N-(1,3-benzothiazol-2-yl)-2-[[5-(pyridin-3-yl)-1,3,4-oxadiazol-2-yl]sulfanyl]acetamide
pH and temperature not specified in the publication
0.0014
N-(1,3-benzothiazol-2-yl)-2-[[5-(pyridin-3-yl)-1,3,4-thiadiazol-2-yl]sulfanyl]acetamide
pH and temperature not specified in the publication
0.00086
N-(1,3-benzothiazol-2-yl)-2-[[5-(pyridin-3-yl)-4H-1,2,4-triazol-3-yl]sulfanyl]acetamide
pH and temperature not specified in the publication
0.00082
N-(1,3-benzothiazol-2-yl)-2-[[5-(pyridin-4-yl)-1,3,4-oxadiazol-2-yl]sulfanyl]acetamide
pH and temperature not specified in the publication
0.00033
N-(1,3-benzothiazol-2-yl)-2-[[5-(pyridin-4-yl)-1,3,4-thiadiazol-2-yl]sulfanyl]acetamide
pH and temperature not specified in the publication
0.00034
N-(1,3-benzothiazol-2-yl)-2-[[5-(pyridin-4-yl)-4H-1,2,4-triazol-3-yl]sulfanyl]acetamide
pH and temperature not specified in the publication
0.00043 - 0.00051
N-phenyl-2-[[5-(pyridin-4-yl)-1,3,4-oxadiazol-2-yl]sulfanyl]acetamide
0.00038 - 0.00039
N-phenyl-2-[[5-(pyridin-4-yl)-1,3,4-thiadiazol-2-yl]sulfanyl]acetamide
0.00025 - 0.00054
N-phenyl-2-[[5-(pyridin-4-yl)-4H-1,2,4-triazol-3-yl]sulfanyl]acetamide
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.4
isoelectric focusing, pH-range 3-10. Basic beta-lactamases (pI: 7.0) and the acid beta-lactamase with pI 5.4 are encoded by the same L2 gene, the active types of these L2 charge variants are dependent on the buffer pH. The L2 charge variants give Stenotrophomonas maltophilia a better chance of adapting and surviving in response to changes in the environment
7
isoelectric focusing, pH-range 3-10. Basic beta-lactamases (pI: 7.0) and the acid beta-lactamase with pI 5.4 are encoded by the same L2 gene, the active types of these L2 charge variants are dependent on the buffer pH. The L2 charge variants give Stenotrophomonas maltophilia a better chance of adapting and surviving in response to changes in the environment
7.1
-
isoelectric focusing
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
the enzyme is a metallo-beta-lactamase of subgroup B3
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
Q9RBQ1_STEMA
303
0
31999
TrEMBL
-
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
28800
-
gel filtration
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
tetramer
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
hanging drop vapour diffusion method with 100 mM HEPES (pH 7.75), 1.8 M (NH4)2SO4, 1.5% (v/v) PEG400
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D120C
site-directed mutagenesis, reduced activity and metal binding compared to the wild-type enzyme
D120N
site-directed mutagenesis, reduced activity and metal binding compared to the wild-type enzyme
D120S
site-directed mutagenesis, reduced activity and metal binding compared to the wild-type enzyme
H116C
site-directed mutagenesis. Mutant binds 0.33 equiv of Zn2+
H118C
site-directed mutagenesis
H121C
site-directed mutagenesis. Mutant binds 0.11 equiv of Zn2+
H196C
site-directed mutagenesis
additional information
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
Q Sepharose column chromatography, SP-Sepharose column chromatography, and gel filtration
recombinant wild-type and mutant enzymes from Escherichia coli
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli
-
expressed in Escherichia coli strain BL21 Star (DE3)
expression of wild-type and mutant enzymes in Escherichia coli
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Crowder, M.W.; Walsh, T.R.; Banovic, L.; Pettit, M.; Spencer, J.
Overexpression, purification, and characterization of the cloned metallo-beta-lactamase L1 from Stenotrophomonas maltophilia
Antimicrob. Agents Chemother.
42
921-926
1998
Stenotrophomonas maltophilia
Manually annotated by BRENDA team
Denny, B.J.; Lambert, P.A.; West, P.W.J.
The flavonoid galangin inhibits the L1 metallo-beta-lactamase from Stenotrophomonas maltophilia
FEMS Microbiol. Lett.
208
21-24
2002
Stenotrophomonas maltophilia
Manually annotated by BRENDA team
Garrity, J.D.; Carenbauer, A.L.; Herron, L.R.; Crowder, M.W.
Metal binding Asp-120 in metallo-beta-lactamase L1 from Stenotrophomonas maltophilia plays a crucial role in catalysis
J. Biol. Chem.
279
920-927
2004
Stenotrophomonas maltophilia (P52700), Stenotrophomonas maltophilia
Manually annotated by BRENDA team
Simm, A.M.; Loveridge, E.J.; Crosby, J.; Avison, M.B.; Walsh, T.R.; Bennett, P.M.
Bulgecin A: a novel inhibitor of binuclear metallo-beta-lactamases
Biochem. J.
387
585-590
2005
Bacillus cereus, Aeromonas veronii, Stenotrophomonas maltophilia (P52700), Stenotrophomonas maltophilia
Manually annotated by BRENDA team
Sanschagrin, F.; Levesque, R.C.
A specific peptide inhibitor of the class B metallo-beta-lactamase L-1 from Stenotrophomonas maltophilia identified using phage display
J. Antimicrob. Chemother.
55
252-255
2005
Stenotrophomonas maltophilia
Manually annotated by BRENDA team
Nauton, L.; Kahn, R.; Garau, G.; Hernandez, J.F.; Dideberg, O.
Structural insights into the design of inhibitors for the L1 metallo-beta-lactamase from Stenotrophomonas maltophilia
J. Mol. Biol.
375
257-269
2008
Stenotrophomonas maltophilia (P52700), Stenotrophomonas maltophilia
Manually annotated by BRENDA team
Hu, R.; Huang, K.; Wu, L.; Hsiao, Y.; Yang, T.
Induction of L1 and L2 beta -lactamases of Stenotrophomonas maltophilia
Antimicrob. Agents Chemother.
52
1198-1200
2008
Stenotrophomonas maltophilia (B1NLE9), Stenotrophomonas maltophilia (Q9RBQ1), Stenotrophomonas maltophilia KJ (B1NLE9), Stenotrophomonas maltophilia KJ (Q9RBQ1)
Manually annotated by BRENDA team
Hu, Z.; Periyannan, G.; Bennett, B.; Crowder, M.W.
Role of the Zn1 and Zn2 sites in Metallo-beta -lactamase L1
J. Am. Chem. Soc.
130
14207-14216
2008
Stenotrophomonas maltophilia (P52700)
Manually annotated by BRENDA team
Hu, R.M.; Chiang, K.H.; Chang, Y.C.; Yang, T.C.
Characterization of the charge variants of L2 beta-lactamase in Stenotrophomonas maltophilia
J. Med. Microbiol.
58
318-321
2009
Stenotrophomonas maltophilia (B5KLI1), Stenotrophomonas maltophilia
Manually annotated by BRENDA team
Zhang, Y.L.; Yang, K.W.; Zhou, Y.J.; LaCuran, A.E.; Oelschlaeger, P.; Crowder, M.W.
Diaryl-substituted azolylthioacetamides: Inhibitor discovery of New Delhi metallo-beta-lactamase-1 (NDM-1)
ChemMedChem
9
2445-2448
2014
Aeromonas veronii, Aeromonas veronii (O31272), Stenotrophomonas maltophilia (E9RIT0), Stenotrophomonas maltophilia, Bacteroides fragilis (P25910), Bacteroides fragilis
Manually annotated by BRENDA team