Purification and characterization of PBP4a, a new low-molecular-weight penicillin-binding protein from Bacillus subtilis - Wikidata - awgldk - TriplyDB

Purification and characterization of PBP4a, a new low-molecular-weight penicillin-binding protein from Bacillus subtilis

Purification and characterization of PBP4a, a new low-molecular-weight penicillin-binding protein from Bacillus subtilis

http://www.wikidata.org/entity/Q33995668

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Crystal Structures of Complexes of Bacterial dd-Peptidases with Peptidoglycan-Mimetic Ligands: The Substrate Specificity Puzzle Inhibition of dd -Peptidases by a Specific Trifluoroketone: Crystal Structure of a Complex with the Actinomadura R39 dd -Peptidase A Lysine Cluster in Domain II of Bacillus subtilis PBP4a Plays a Role in the Membrane Attachment of This C1-PBP Substrate-induced inactivation of the Escherichia coli AmiD N-acetylmuramoyl-L-alanine amidase highlights a new strategy to inhibit this class of enzyme On the substrate specificity of bacterial DD-peptidases: evidence from two series of peptidoglycan-mimetic peptides Biosynthetic pathway for mannopeptimycins, lipoglycopeptide antibiotics active against drug-resistant gram-positive pathogens Crystal structure of the Actinomadura R39 DD-peptidase reveals new domains in penicillin-binding proteins.

P2860

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P2860

Purification and characterization of PBP4a, a new low-molecular-weight penicillin-binding protein from Bacillus subtilis

http://www.wikidata.org/entity/Q33995668

description

2001 nî lūn-bûn

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2001 թուականի Մարտին հրատարակուած գիտական յօդուած

@hyw

2001 թվականի մարտին հրատարակված գիտական հոդված

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2001年の論文

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2001年論文

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2001年論文

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2001年論文

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2001年論文

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2001年論文

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2001年论文

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Purification and characterizat ...... protein from Bacillus subtilis

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Purification and characterizat ...... protein from Bacillus subtilis

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Purification and characterizat ...... protein from Bacillus subtilis

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Purification and characterizat ...... protein from Bacillus subtilis

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prefLabel

Purification and characterizat ...... protein from Bacillus subtilis

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Purification and characterizat ...... protein from Bacillus subtilis

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JB.183.5.1595-1599.2001

P1433

Journal of Bacteriology

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Purification and characterizat ...... protein from Bacillus subtilis

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P2093

A Brans

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

C Duez

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F Bouillenne

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J Docquier

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J Frère

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M Vanhove

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X Gallet

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P2860

The complete genome sequence of the gram-positive bacterium Bacillus subtilis

A comprehensive set of sequence analysis programs for the VAX

Whole-genome random sequencing and assembly of Haemophilus influenzae Rd

Interaction of beta-iodopenicillanate with the beta-lactamases of Streptomyces albus G and Actinomadura R39

Roles of low-molecular-weight penicillin-binding proteins in Bacillus subtilis spore peptidoglycan synthesis and spore properties.

Characterization of dacC, which encodes a new low-molecular-weight penicillin-binding protein in Bacillus subtilis.

Penicillin-sensitive enzymes in peptidoglycan biosynthesis.

A second regulatory gene, blaR1, encoding a potential penicillin-binding protein required for induction of beta-lactamase in Bacillus licheniformis.

Beta-lactamase as a probe of membrane protein assembly and protein export.

Penicillinase from Bacillus licheniformis: nucleotide sequence of the gene and implications for the biosynthesis of a secretory protein in a Gram-positive bacterium.

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1595-1599

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scholarly article

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10.1128/JB.183.5.1595-1599.2001

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5

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183

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2001-03-01T00:00:00Z

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12169831

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11160090

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95044

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