Literature summary for 3.5.1.28 extracted from

Chaput, C.; Ecobichon, C.; Pouradier, N.; Rousselle, J.C.; Namane, A.; Boneca, I.G.
Role of the N-acetylmuramoyl-L-alanyl amidase, AmiA, of Helicobacter pylori in peptidoglycan metabolism, daughter cell separation, and virulence (2016), Microb. Drug Resist., 22, 477-486 .

Search for more literature for 3.5.1.28

Localization

Localization	Comment	Organism	GeneOntology No.	Textmining
cell wall	-	Helicobacter pylori	5618	-
periplasm	-	Helicobacter pylori	-	-

Organism

Organism	UniProt	Comment	Textmining
Helicobacter pylori	O25464	-	-
Helicobacter pylori 26695	O25464	-	-
Helicobacter pylori ATCC 700392	O25464	-	-

Synonyms

Synonyms	Comment	Organism
AmiA	-	Helicobacter pylori

General Information

General Information	Comment	Organism
malfunction	analysis of peptidoglycan (PG) muropeptide composition and glycan chain length distribution of wild-type strain 26695 and its amiA mutant: the analysis shows that Helicobacter pylori lacks muropeptides with a degree of cross-linking higher than dimeric muropeptides. The amiA mutant is also characterized by a decrease of muropeptides carrying 1,6-anhydro-N-acetylmuramic acid residues, which represent the ends of the glycan chains. This correlated with an increase of very long glycan strands in the amiA mutant. Modifications in PG composition of amiA mutant, overview. The susceptibility of the cells to different antibiotics is unaltered in the amiA mutant cells compared to wild-type cells	Helicobacter pylori
additional information	analysis of peptidoglycan muropeptide composition and glycan chain length distribution, overview	Helicobacter pylori

Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.

Release 2023.1 (January 2023)