⌘+K

Pulse Explore Communities Researchers Journals

Home Communities Explore

July 1, 1976Journal of BacteriologyOpen Access

Identification of the Major Penicillin-Binding Proteins of Escherichia coli as d -Alanine Carboxypeptidase IA

Brian G. Spratt Jack L. Strominger

View Full Paper

Ask AI

Bookmark

Share

Abstract

Penicillin-binding proteins 5 and 6 of Escherichia coli have been identified as d-alanine carboxypeptidase IA.

Discussion

No takes yet. Share an insight, caveat, or question.

Cite This Study

Spratt et al. (1976) studied this question.

synapsesocial.com/papers/6a7180cef44fa9f079df4a82 https://doi.org/10.1128/jb.127.1.660-663.1976

View Full Paper

Ask AI

Bookmark

Share

Keep reading

Synapse has enriched 5 related papers. Consider them for comparative context:

1Fractionation of the DD‐Carboxypeptidase‐Transpeptidase Activities Solubilized from Membranes of Escherichia coli K12, Strain 44Original Research · 1974 · 48 citations
2Distinct penicillin binding proteins involved in the division, elongation, and shape of Escherichia coli K12.Original Research · 1975 · 974 citations
3Purification to homogeneity and properties of two D-alanine carboxypeptidases I From Escherichia coli.Original Research · 1976 · 145 citations
4Structural and biochemical insights into isophthalate dihydrodiol dehydrogenase from Comamonas testosteroni KF1Journal of Bacteriology · Wed,
5Anabaena , a multicellular model for cyanobacterial cell biology and biotechnologyJournal of Bacteriology · Tue,

More from Journal of Bacteriology

A transcriptional repressor co-regulatory network integrates iron homeostasis and mycobacterial stress tolerance to oxidative stressTue,
Contribution of PonA2 to biofilm and colony formation independent of its catalytic domains in Mycobacterium smegmatisWed,
Molecular mechanisms and regulatory networks governing Yersinia biofilm formation and host adaptationTue,
The evolution of Brucella as a model intracellular pathogenTue,
The virulence regulator ToxT influences Vibrio cholerae motility through the expression of the methyl-accepting chemoreceptors AcfB and TcpITue,