Efficient catalysis by beta-lactamase from Staphylococcus aureus PC1 accompanied by accumulation of an acyl-enzyme.

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Identification of a β-lactamase inhibitory protein variant that is a potent inhibitor of Staphylococcus PC1 β-lactamase.Electrostatic steering and ionic tethering in enzyme-ligand binding: insights from simulations.

P2860

Q33794586-23A6B241-21A4-4C3F-966D-97417197FB36 Q36159830-D06F8989-B9F3-4145-AB16-A451CEB20DFD

P2860

Efficient catalysis by beta-lactamase from Staphylococcus aureus PC1 accompanied by accumulation of an acyl-enzyme.

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http://www.wikidata.org/entity/Q41828188

description

1996 nî lūn-bûn

@nan

1996年の論文

@ja

1996年論文

@yue

1996年論文

@zh-hant

1996年論文

@zh-hk

1996年論文

@zh-mo

1996年論文

@zh-tw

1996年论文

@wuu

1996年论文

@zh

1996年论文

@zh-cn

name

Efficient catalysis by beta-la ...... ccumulation of an acyl-enzyme.

@en

type

Item

label

Efficient catalysis by beta-la ...... ccumulation of an acyl-enzyme.

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prefLabel

Efficient catalysis by beta-la ...... ccumulation of an acyl-enzyme.

@en

P1476

Efficient catalysis by beta-la ...... ccumulation of an acyl-enzyme.

@en

P2093

Qi X

http://www.w3.org/2001/XMLSchema#string

Virden R

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P2860

Structural basis for the inactivation of the P54 mutant of beta-lactamase from Staphylococcus aureus PC1

Refined crystal structure of beta-lactamase from Staphylococcus aureus PC1 at 2.0 A resolution

Evidence for two acyl group conformations in some furylacryloyl- and thienylacryloylchymotrypsins: resonance Raman studies of enzyme--substrate intermediates at pH 3.0.

Effects of site-specific mutagenesis of tyrosine 105 in a class A beta-lactamase.

N-(2-Furyl) acryloyl penicillin: a novel compound for the spectrophotometric assay of beta-lactamase I.

The enigmatic catalytic mechanism of active-site serine beta-lactamases.

Reversible deactivation of beta-lactamase by quinacillin. Extent of the conformational change in the isolated transitory complex.

Beta-lactamases as fully efficient enzymes. Determination of all the rate constants in the acyl-enzyme mechanism.

The mechanism of folding of globular proteins. Suitability of a penicillinase from Staphylococcus Aureus as a model for refolding studies

Kinetic parameters of the acyl-enzyme mechanism and conditions for quasi-equilibrium and for optimal catalytic characteristics.

P304

537-541

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P31

scholarly article

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10.1042/BJ3150537

http://www.w3.org/2001/XMLSchema#string

P407

English

P478

315 ( Pt 2)

http://www.w3.org/2001/XMLSchema#string

P577

1996-04-01T00:00:00Z

http://www.w3.org/2001/XMLSchema#dateTime

P5875

14584384

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P698

8615826

http://www.w3.org/2001/XMLSchema#string

P932

1217229

http://www.w3.org/2001/XMLSchema#string

Efficient catalysis by beta-lactamase from Staphylococcus aureus PC1 accompanied by accumulation of an acyl-enzyme.

about

P2860

P2860

Efficient catalysis by beta-lactamase from Staphylococcus aureus PC1 accompanied by accumulation of an acyl-enzyme.

description

name

type

label

prefLabel

P1433

P1476

P2093

P2860

P304

P31

P356

P407

P478

P577

P5875

P698

P932

P356

P1433

P1476

P2093

P2860

P304

P31

P356

P407

P478

P577

P5875

P698

P932