Information on EC 3.2.1.B37 - N-acetylmuramoyl-glycoprotein endo-beta-N-acetylglucosaminidase

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The expected taxonomic range for this enzyme is: Clostridioides difficile

EC NUMBER
COMMENTARY hide
3.2.1.B37
preliminary BRENDA-supplied EC number
RECOMMENDED NAME
GeneOntology No.
N-acetylmuramoyl-glycoprotein endo-beta-N-acetylglucosaminidase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
4-O-N-acetyl-beta-D-glucosaminyl-N-acetylmuramoyl-[glycoprotein] + H2O = N-acetylmuramoyl-[glycoprotein] + N-acetyl-D-glucosamine
show the reaction diagram
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SYSTEMATIC NAME
IUBMB Comments
N-acetylmuramoyl-glycoprotein N-acetyl-D-glucosamine hydrolase
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
enzyme is a cell-wall hydrolase with lytic activity on the peptidoglycan of several Gram-positive bacteria, including Clostridium difficile. Enzyme hydrolyses peptidoglycan bonds between N-acetylglucosamine and N-acetylmuramic acid
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
Bacillus subtilis 168 HR cell wall + H2O
soluble muropeptides
show the reaction diagram
enzyme hydrolyses peptidoglycan bonds between N-acetylglucosamine and N-acetylmuramic acid. Enzyme does not possess muraminidase activity
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?
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
64000
x * 65852, calculated, x * 64000, SDS-PAGE
65852
x * 65852, calculated, x * 64000, SDS-PAGE
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
x * 65852, calculated, x * 64000, SDS-PAGE
additional information
deduced amino acid sequence of Acd shows a modular structure with an N-terminal domain exhibiting repeated sequences and a C-terminal catalytic domain
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
proteolytic modification
first 22 N-terminal residues of the protein encode a putative signal sequence or an N-terminal signal anchor sequence
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
transcription of the Acd gene increases during vegetative cellular growth