Point mutations of two arginine residues in the Streptomyces R61 DD-peptidase.

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Site-directed mutagenesis of the Streptomyces R61 DD-peptidase. Catalytic function of the conserved residues around the active site and a comparison with class-A and class-C beta-lactamases.The precursor of the Streptomyces R61 DD-peptidase containing a C-terminal extension is inactive.

P2860

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P2860

Point mutations of two arginine residues in the Streptomyces R61 DD-peptidase.

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http://www.wikidata.org/entity/Q42099606

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1992 nî lūn-bûn

@nan

1992年の論文

@ja

1992年論文

@yue

1992年論文

@zh-hant

1992年論文

@zh-hk

1992年論文

@zh-mo

1992年論文

@zh-tw

1992年论文

@wuu

1992年论文

@zh

1992年论文

@zh-cn

name

Point mutations of two arginine residues in the Streptomyces R61 DD-peptidase.

@en

Point mutations of two arginine residues in the Streptomyces R61 DD-peptidase.

@nl

type

Item

label

Point mutations of two arginine residues in the Streptomyces R61 DD-peptidase.

@en

Point mutations of two arginine residues in the Streptomyces R61 DD-peptidase.

@nl

prefLabel

Point mutations of two arginine residues in the Streptomyces R61 DD-peptidase.

@en

Point mutations of two arginine residues in the Streptomyces R61 DD-peptidase.

@nl

P1476

Point mutations of two arginine residues in the Streptomyces R61 DD-peptidase.

@en

P2093

Bourguignon-Bellefroid C

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

Frère JM

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

Ghuysen JM

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Joris B

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Van Beeumen J

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P2860

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

Beta-lactamase of Bacillus licheniformis 749/C at 2 A resolution

Penicillin-sensitive enzymes in peptidoglycan biosynthesis.

Site-saturation studies of beta-lactamase: production and characterization of mutant beta-lactamases with all possible amino acid substitutions at residue 71

Primary structure of the Streptomyces R61 extracellular DD-peptidase. 2. Amino acid sequence data.

Penicillin-resistant isolates of Neisseria lactamica produce altered forms of penicillin-binding protein 2 that arose by interspecies horizontal gene transfer.

Role of the conserved amino acids of the 'SDN' loop (Ser130, Asp131 and Asn132) in a class A beta-lactamase studied by site-directed mutagenesis.

beta-lactamase I from Bacillus cereus. Structure and site-directed mutagenesis.

Unusual septum formation in Streptococcus pneumoniae mutants with an alteration in the D,D-carboxypeptidase penicillin-binding protein 3.

Accumulation of acyl-enzyme in DD-peptidase-catalysed reactions with analogues of peptide substrates.

P304

123-128

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P31

scholarly article

P356

10.1042/BJ2830123

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P407

English

P478

283 ( Pt 1)

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P577

1992-04-01T00:00:00Z

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P5875

21589087

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P698

1567359

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P932

1131003

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Point mutations of two arginine residues in the Streptomyces R61 DD-peptidase.

about

P2860

P2860

Point mutations of two arginine residues in the Streptomyces R61 DD-peptidase.

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