EzCatDB: S00535
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DB codeS00535
CATH domainDomain 13.40.80.10 : Lysozyme-likeCatalytic domain
E.C.3.5.1.28

CATH domainRelated DB codes (homologues)
3.40.80.10 : Lysozyme-likeS00502,S00536

Enzyme Name
UniProtKBKEGG

P82974
Protein name1,6-anhydro-N-acetylmuramyl-L-alanine amidase ampDN-acetylmuramoyl-L-alanine amidase
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
murein hydrolase
N-acetylmuramoyl-L-alanine amidase type I
N-acetylmuramoyl-L-alanine amidase type II
SynonymsEC 3.5.1.28
N-acetylmuramoyl-L-alanine amidase
PfamPF01510 (Amidase_2)
[Graphical view]

KEGG pathways
MAP codePathways
MAP00550Peptidoglycan biosynthesis

UniProtKB:Accession NumberP82974
Entry nameAMPD_CITFR
Activity
Subunit
Subcellular locationCytoplasm (By similarity).
Cofactor

Compound table: links to PDB-related databases & PoSSuM

CofactorsSubstratesProducts
KEGG-idC00038L00022C00001C05887C00012
CompoundZincGlycopeptide containing N-acetylmuramoyl-peptideH2ON-Acetyl-D-muramoatePeptide
Typeheavy metalamide group,peptide/protein,polysaccharideH2Oamide group,carbohydrate,carboxyl grouppeptide/protein
ChEBI29105

15377


PubChem32051

962
22247451


             
1iyaABound:_ZNUnbound UnboundUnbound
1j2sABound:_ZNUnbound UnboundUnbound
1j3gABound:_ZNUnbound UnboundUnbound

Active-site residues
resource
literature [8], [10]
pdbCatalytic residuesCofactor-binding residues
          
1iyaATYR 63;HIS 96;GLU 116;LYS 162
HIS 34;HIS 154;ASP 164
1j2sATYR 63;HIS 96;GLU 116;LYS 162
HIS 34;HIS 154;ASP 164
1j3gATYR 63;HIS 96;GLU 116;LYS 162
HIS 34;HIS 154;ASP 164

References for Catalytic Mechanism
ReferencesSectionsNo. of steps in catalysis
[2]p.4037
[8]p.836-838
[9]p.789-791
[10]Scheme 1, p.118-1193
[11]p.35435-35439

references
[1]
PubMed ID4582731
JournalJ Biol Chem
Year1973
Volume248
Pages7247-52
AuthorsInouye M, Arnheim N, Sternglanz R
TitleBacteriophage T7 lysozyme is an N-acetylmuramyl-L-alanine amidase.
[2]
CommentsX-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS), AND REVISION TO 118.
Medline ID94224877
PubMed ID8171031
JournalProc Natl Acad Sci U S A
Year1994
Volume91
Pages4034-8
AuthorsCheng X, Zhang X, Pflugrath JW, Studier FW
TitleThe structure of bacteriophage T7 lysozyme, a zinc amidase and an inhibitor of T7 RNA polymerase.
Related PDB1lba
Related UniProtKBP00806
[3]
PubMed ID9405156
JournalJ Mol Biol
Year1997
Volume274
Pages748-56
AuthorsJeruzalmi D, Steitz TA
TitleUse of organic cosmotropic solutes to crystallize flexible proteins: application to T7 RNA polymerase and its complex with the inhibitor T7 lysozyme.
[4]
CommentsX-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF COMPLEX WITH POLYMERASE.
Medline ID98336199
PubMed ID9670025
JournalEMBO J
Year1998
Volume17
Pages4101-13
AuthorsJeruzalmi D, Steitz TA
TitleStructure of T7 RNA polymerase complexed to the transcriptional inhibitor T7 lysozyme.
Related PDB1aro
Related UniProtKBP00806
[5]
PubMed ID9719635
JournalJ Mol Biol
Year1998
Volume281
Pages793-802
AuthorsVillemain J, Sousa R
TitleSpecificity in transcriptional regulation in the absence of specific DNA binding sites: the case of T7 lysozyme.
[6]
PubMed ID10543943
JournalJ Mol Biol
Year1999
Volume293
Pages457-75
AuthorsHuang J, Villemain J, Padilla R, Sousa R
TitleMechanisms by which T7 lysozyme specifically regulates T7 RNA polymerase during different phases of transcription.
[7]
PubMed ID10679468
JournalCurr Opin Struct Biol
Year2000
Volume10
Pages117-23
AuthorsCheetham GM, Steitz TA
TitleInsights into transcription: structure and function of single-subunit DNA-dependent RNA polymerases.
[8]
PubMed ID12654266
JournalJ Mol Biol
Year2003
Volume327
Pages833-42
AuthorsLiepinsh E, Genereux C, Dehareng D, Joris B, Otting G
TitleNMR structure of Citrobacter freundii AmpD, comparison with bacteriophage T7 lysozyme and homology with PGRP domains.
Related PDB1iya,1j2s
[9]
PubMed ID12845326
JournalNat Immunol
Year2003
Volume4
Pages787-93
AuthorsKim MS, Byun M, Oh BH
TitleCrystal structure of peptidoglycan recognition protein LB from Drosophila melanogaster.
Related PDB1oht
[10]
PubMed ID14507260
JournalBiochem J
Year2004
Volume377
Pages111-20
AuthorsGenereux C, Dehareng D, Devreese B, Van Beeumen J, Frere JM, Joris B
TitleMutational analysis of the catalytic centre of the Citrobacter freundii AmpD N-acetylmuramyl-L-alanine amidase.
[11]
PubMed ID16103125
JournalJ Biol Chem
Year2005
Volume280
Pages35433-9
AuthorsLow LY, Yang C, Perego M, Osterman A, Liddington RC
TitleStructure and lytic activity of a Bacillus anthracis prophage endolysin.

comments
This enzyme is homologous to bacteriophage T7 lysozyme (S00502 in EzCatDB) and PGRPs(S00536). However, the catalytic residues are not completely the same as those by its homologues.
Instead of Tyr48 as a general base-acid in T7 lysozyme, it is not clear which of residues, Tyr63, His96 or Glu116, can acts as a general base-acid in this enzyme (see [8] and [10]).

createdupdated
2004-05-112009-02-26


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