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Information on EC 3.2.1.17 - lysozyme and Organism(s) Meretrix lusoria and UniProt Accession P86383

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EC Tree
     3 Hydrolases
         3.2 Glycosylases
             3.2.1 Glycosidases, i.e. enzymes that hydrolyse O- and S-glycosyl compounds
                3.2.1.17 lysozyme
IUBMB Comments
cf. also EC 3.2.1.14 chitinase.
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This record set is specific for:
Meretrix lusoria
UNIPROT: P86383
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Word Map
The taxonomic range for the selected organisms is: Meretrix lusoria
The enzyme appears in selected viruses and cellular organisms
Synonyms
lysozyme, endolysin, autolysin, t4 lysozyme, transglycosylase, muramidase, peptidoglycan hydrolase, lysozyme a, mutanolysin, lysozyme c, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
i-type lysozyme
-
1,4-beta-N-acetylmuramidase
-
-
-
-
1,4-beta-N-acetylmuramidase A/C
-
-
-
-
1,4-beta-N-acetylmuramidase M1
-
-
-
-
1,4-beta-N-acetylmuramoylhydrolase
-
-
-
-
1,4-N-acetylmuramidase
-
-
-
-
Autolysin
-
-
-
-
CP-1 lysin
-
-
-
-
CP-7 lysin
-
-
-
-
CP-9 lysin
-
-
-
-
CPL
-
-
-
-
endolysin
-
-
-
-
globulin G
-
-
-
-
globulin G1
-
-
-
-
Goose-type lysozyme
-
-
-
-
L-7001
-
-
-
-
Late protein gp15
-
-
-
-
Lysis protein
-
-
-
-
Lysosyme
-
-
-
-
Lysozyme
-
-
-
-
lysozyme g
-
-
-
-
mucopeptide glucohydrolase
-
-
-
-
mucopeptide N-acetylmuramoylhydrolase
-
-
-
-
muramidase
-
-
-
-
MV1 lysin
-
-
-
-
N,O-diacetylmuramidase
-
-
-
-
Outer wedge of baseplate protein
-
-
-
-
P13
-
-
-
-
Peptidoglycan hydrolase
-
-
-
-
PR1-lysozyme
-
-
-
-
Protein gp17
-
-
-
-
Protein gp19
-
-
-
-
Protein Gp25
-
-
-
-
Protein Gp5
-
-
-
-
Protein gp54
-
-
-
-
Protein gpK
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of O-glycosyl bond
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
peptidoglycan N-acetylmuramoylhydrolase
cf. also EC 3.2.1.14 chitinase.
CAS REGISTRY NUMBER
COMMENTARY hide
9001-63-2
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
chitohexaose + H2O
?
show the reaction diagram
-
-
-
?
chitopentaose + H2O
?
show the reaction diagram
-
-
-
?
lyophilized cell wall of Micrococcus luteus + H2O
?
show the reaction diagram
-
-
-
?
additional information
?
-
the enzyme shows also chitinase activity on glycol chitin as substrate, but no transglycosylation activity, and a higher number of subsites compared to hen egg-white enzyme
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
no increase in activity at high ionic strength
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
1227
purified lysozyme B, pH 7.0, 25°C
620
purified lysozyme A, pH 7.0, 25°C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5
assay at, substrate N-acetylglucosamine oligomers
6.5
substrate lyophilized cell wall of Micrococcus luteus, isozyme lysozyme A
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
25
assay at, lytic activity, substrate lyophilized cell wall of Micrococcus luteus
50
assay at, substrate N-acetylglucosamine oligomers
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
i-type lysozyme, two isozymes lysozyme A and lysozyme B
UniProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
structure-function relationhip of two isozymes of the invertebrate i-type lysozyme, active site residues are Glu18 and Asp30, substrate interaction via residues P44, Y45, Y47, H94, and p98, overview
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
LYS_MERLU
122
0
13377
Swiss-Prot
other Location (Reliability: 3)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
13363
1 * 14000, lysozymes A and B, SDS-PAGE, 1 * 13382, lysozyme A, sequence calculation 1 * 13376, lysozyme A, mass spectrometry, 1 * 13363, lysozyme B, mass spectrometry
13376
1 * 14000, lysozymes A and B, SDS-PAGE, 1 * 13382, lysozyme A, sequence calculation 1 * 13376, lysozyme A, mass spectrometry, 1 * 13363, lysozyme B, mass spectrometry
13382
1 * 14000, lysozymes A and B, SDS-PAGE, 1 * 13382, lysozyme A, sequence calculation 1 * 13376, lysozyme A, mass spectrometry, 1 * 13363, lysozyme B, mass spectrometry
14000
1 * 14000, lysozymes A and B, SDS-PAGE, 1 * 13382, lysozyme A, sequence calculation 1 * 13376, lysozyme A, mass spectrometry, 1 * 13363, lysozyme B, mass spectrometry
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
1 * 14000, lysozymes A and B, SDS-PAGE, 1 * 13382, lysozyme A, sequence calculation 1 * 13376, lysozyme A, mass spectrometry, 1 * 13363, lysozyme B, mass spectrometry
additional information
the enzyme shows no dimerization like the enzyme of bivalve Venerupis philippinarum due to the lack of residue Lys108 responsible of dimerization in the other organism
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
native isozymes to homogeneity by ammonium sulfate fractionation, two steps of cation exchange chromatography, and isozyme separation by reversed phase gel filtration
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic analysis
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Kuwano, Y.; Yoneda, K.; Kawaguchi, Y.; Araki, N.; Araki, T.
The complete amino acid sequence and enzymatic properties of an i-type lysozyme isolated from the common orient clam (Meretrix lusoria)
Biosci. Biotechnol. Biochem.
77
2269-2277
2013
Meretrix lusoria (P86383)
Manually annotated by BRENDA team