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Information on EC 4.2.2.B6 - muropeptide lyase

for references in articles please use BRENDA:EC4.2.2.B6
preliminary BRENDA-supplied EC number
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EC Tree
     4 Lyases
         4.2 Carbon-oxygen lyases
             4.2.2 Acting on polysaccharides
                4.2.2.B6 muropeptide lyase
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This record set is specific for:
UNIPROT: P0C960
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The enzyme appears in viruses and cellular organisms
Synonyms
endolytic peptidoglycan lytic transglycosylase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
endolytic peptidoglycan lytic transglycosylase
-
GlcNAc-beta-(1->4)-Mur2Acoyl-L-Ala-gamma-D-Glu lyase (1,6-anhydromuramoyl-residue forming)
systematic name
muropeptide lyase
recommended name
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
Micrococcus luteus peptidoglycan
?
show the reaction diagram
-
-
-
?
additional information
?
-
the enzyme cleaves the beta-1,4-glycosidic bonds between N-acetylmuramic acid and N-acetylglucosamine residues in the cell wall peptidoglycan, producing 1,6-anhydromuropeptides
-
-
?
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
UniProt
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
a periplasmic, outer membrane-attached enzyme
Manually annotated by BRENDA team
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
EMTA_ECOLI
Escherichia coli (strain K12)
203
0
22227
Swiss-Prot
Secretory Pathway (Reliability: 4)
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
in solution, the enzyme behaves as a monomer, as judged from size exclusion chromatography and dynamic light scattering
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
in complex with the glycopeptide inhibitor bulgecin A and N-acetylglucosaminyl-N-acetylmuramyl-L-Ala-D-Glu, hanging drop vapor diffusion method, using 0.1 M lithium sulfate, 15% (w/v) PEG 8000 in 20 mM HEPES buffer, pH 7.5
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
Ni-NTA column chromatography
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
mutant enzyme E64Q is expressed in Escherichi coli strain B834(DE3) pLysS
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Fibriansah, G.; Gliubich, F.I.; Thunnissen, A.M.
on the mechanism of peptidoglycan binding and cleavage by the endo-specific lytic transglycosylase MltE from Escherichia coli
Biochemistry
51
9164-9177
2012
Escherichia coli (P0C960)
Manually annotated by BRENDA team