Literature summary for 3.5.2.6 extracted from

Fonze, E.; Vanhove, M.; Dive, G.; Sauvage, E.; Frere, J.M.; Charlier, P.
Crystal structures of the Bacillus licheniformis BS3 class A beta-lactamase and of the acyl-enzyme adduct formed with cefoxitin (2002), Biochemistry, 41, 1877-1885.

Crystallization (Commentary)

Crystallization (Comment)	Organism
purified recombinant enzyme, complexed with cefoxitin in an acyl-enzyme-adduct, for monoclinic crystals: 0.005 ml protein solution, 10 mg/ml, + equal volume of reservoir solution containing 25% PEG 6000, 0.1 M sodium acetate, pH 5.0, against 1 ml of reservoir solution at 20°C, for very big prismatic crystals: 40 mg/ml protein with lowered PEG 6000 concentration, pH 3.4, complexing by diffusion of cefoxitin for 24 h, X-ray diffraction structure determination and analysis at 1.7 A resolution	Bacillus licheniformis

Crystallization (Comment)

Organism

purified recombinant enzyme, complexed with cefoxitin in an acyl-enzyme-adduct, for monoclinic crystals: 0.005 ml protein solution, 10 mg/ml, + equal volume of reservoir solution containing 25% PEG 6000, 0.1 M sodium acetate, pH 5.0, against 1 ml of reservoir solution at 20°C, for very big prismatic crystals: 40 mg/ml protein with lowered PEG 6000 concentration, pH 3.4, complexing by diffusion of cefoxitin for 24 h, X-ray diffraction structure determination and analysis at 1.7 A resolution

Bacillus licheniformis

Inhibitors

Inhibitors	Comment	Organism	Structure
cefoxitin	perturbs the active site structure and the conformation of the omega-loop bearing the catalytic residue Glu166, inhibition mechanism	Bacillus licheniformis
additional information	inhibition kinetics	Bacillus licheniformis

KM Value [mM]

KM Value [mM]	KM Value Maximum [mM]	Substrate	Comment	Organism	Structure
additional information	-	additional information	kinetics	Bacillus licheniformis

Organism

Organism	UniProt	Comment	Textmining
Bacillus licheniformis	P00808	class A enzyme BS3	-

Reaction

Reaction	Comment	Organism	Reaction ID
a beta-lactam + H2O = a substituted beta-amino acid	Glu166 is important for catalysis, mechanism	Bacillus licheniformis	a

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.
7-beta-formamidoyl-7-alpha-methoxycephalosporanic acid + H2O	-	Bacillus licheniformis	(2R)-5-[(acetyloxy)methyl]-2-{(S)-carboxy[(E)-(hydroxymethylidene)amino]methoxymethyl}-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid	-	?
a penicillin + H2O	-	Bacillus licheniformis	a penicilloic acid	-	?
cefoxitin + H2O	-	Bacillus licheniformis	(2R)-5-[(carbamoyloxy)methyl]-2-[(S)-carboxy(methoxy)[(thiophen-2-ylacetyl)amino]methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid	-	?
cephalotin + H2O	-	Bacillus licheniformis	(2R)-5-[(acetyloxy)methyl]-2-[(R)-carboxy[(thiophen-2-ylacetyl)amino]methyl]-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid	-	?
moxalactam + H2O	-	Bacillus licheniformis	(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	-	?

Synonyms

Synonyms	Comment	Organism
BS3	-	Bacillus licheniformis

Temperature Optimum [°C]

Temperature Optimum [°C]	Temperature Optimum Maximum [°C]	Comment	Organism
30	-	assay at	Bacillus licheniformis