N-acetylmuramoyl-L-alanine amidase

N-acetylmuramoyl-L-alanine amidase
Identifiers
EC number 3.5.1.28
CAS number 9013-25-6
Databases
IntEnz IntEnz view
BRENDA BRENDA entry
ExPASy NiceZyme view
KEGG KEGG entry
MetaCyc metabolic pathway
PRIAM profile
PDB structures RCSB PDB PDBe PDBsum
Gene Ontology AmiGO / EGO
Amidase_2

crystal structure of the c-terminal peptidoglycan-binding domain of human peptidoglycan recognition protein ialpha
Identifiers
Symbol Amidase_2
Pfam PF01510
InterPro IPR002502
SCOP 1lba
SUPERFAMILY 1lba
OPM superfamily 438
OPM protein 1sk4
Amidase_3

structure of the catalytic domain of cwlv, n-acetylmuramoyl-l-alanine amidase from bacillus(paenibacillus) polymyxa var.colistinus
Identifiers
Symbol Amidase_3
Pfam PF01520
Pfam clan CL0035
InterPro IPR002508
SCOP 1jwq
SUPERFAMILY 1jwq
Amidase_5
Identifiers
Symbol Amidase_5
Pfam PF05382
Pfam clan CL0125
InterPro IPR008044
Amidase02_C
Identifiers
Symbol Amidase02_C
Pfam PF12123
InterPro IPR021976

In enzymology, a N-acetylmuramoyl-L-alanine amidase (EC 3.5.1.28) is an enzyme that catalyzes a chemical reaction that cleaves the link between N-acetylmuramoyl residues and L-amino acid residues in certain cell-wall glycopeptides.

This enzyme belongs to the family of hydrolases, specifically those acting on carbon-nitrogen bonds other than peptide bonds in linear amides. The systematic name of this enzyme class is peptidoglycan amidohydrolase. Other names in common use include acetylmuramyl-L-alanine amidase, N-acetylmuramyl-L-alanine amidase, N-acylmuramyl-L-alanine amidase, acetylmuramoyl-alanine amidase, N-acetylmuramic acid L-alanine amidase, acetylmuramyl-alanine amidase, N-acetylmuramylalanine amidase, N-acetylmuramoyl-L-alanine amidase type I, and N-acetylmuramoyl-L-alanine amidase type II. This enzyme participates in peptidoglycan biosynthesis. Autolysins and some phage lysins are examples of N-acetylmuramoyl-L-alanine amidases.

See also

References

    This article is issued from Wikipedia - version of the 8/10/2016. The text is available under the Creative Commons Attribution/Share Alike but additional terms may apply for the media files.