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Information on EC 3.2.1.17 - lysozyme and Organism(s) Bos taurus and UniProt Accession P80189

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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:
Bos taurus
UNIPROT: P80189
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Word Map
The taxonomic range for the selected organisms is: Bos taurus
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
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
glycol chitin + H2O
chitin oligosaccharides
show the reaction diagram
-
-
-
?
chitotetraose + H2O
chitotriose + N-acetylglucosamine
show the reaction diagram
-
-
-
?
additional information
?
-
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
(GlcNAc)3
-
chitotetraose
-
-
N-acetylglucosamine
-
-
N-acetylmuramic acid
-
-
additional information
-
the enzyme shows resistance to proteolysis
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.5
assay at
4.4
-
-
5 - 8
-
-
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
3 - 7
-
-
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
40
assay at
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.65
-
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
Uniprot
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
3 lysozymes c
Manually annotated by BRENDA team
-
-
Manually annotated by BRENDA team
-
-
Manually annotated by BRENDA team
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
LYSCN_BOVIN
148
0
16476
Swiss-Prot
Secretory Pathway (Reliability: 1)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
14000 - 14850
-
4 isoforms, ion spray mass spectometry
15000
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
-
x * 15000, SDS-PAGE
monomer
-
4 isoforms, 1 * 14100-15000, SDS-PAGE
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant bovine stomach lysozyme 2, to 1.5 A resolution. Space group P212121. Stability may be due to negatively charged surfaces, a shortened loop and slat bridges
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
broad pH stability
729407
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
20 - 70
-
unaffected, 10 min, pH 5.0
62.8
Tm value, pH 2.0
additional information
-
broad thermal stability
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
effects of freezing, thawing and freeze-drying are negligible
-
lysozymes C unusually resistant to inactivation by pepsin
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant enzyme from sugarcane stalks, Saccharum spp. hybrid, extraction condition evaluation and optimization at 22°C, and different pH levels and salt concentrations, overview. pH values greater than 7.5 and salt concentrations higher than 150 mM NaCl do not increase the amount of extracted enzyme. Purification by cross-flow filtration and hydrophobic interaction chromatography.
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant enzyme expression in sugarcane stalks, Saccharum spp. hybrid, process evaluation and optimization, overview
-
RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
Cm value for guanidinium hydrochloride-induced unfolding is 3.1 M at pH 2.0, and 4.2 M at pH 6.0, respectively
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Dobson, D.E.; Prager, E.M.; Wilson, A.C.
Stomach lysozymes of ruminants. I. Distribution and catalytic properties
J. Biol. Chem.
259
11607-11616
1984
Bos taurus, Cervidae, Ovis aries, Ruminantia
Manually annotated by BRENDA team
Pahud, J.J.; Widmer, F.
Calf rennet lysozyme
Biochem. J.
201
661-664
1982
Bos taurus
Manually annotated by BRENDA team
Guenther, H.L.; Sorgente, N.; Guenther, H.E.; Eisenstein, R.; Kuettner, K.E.
Lysozyme in preosseous cartilage. VI. Purification, characterization and localization of mammalian cartilage lysozyme
Biochim. Biophys. Acta
372
321-334
1974
Bos taurus, Canis lupus familiaris
-
Manually annotated by BRENDA team
Ito, Y.; Yamada, H.; Nakamura, M.; Yoshikawa, A.; Ueda, T.; Imoto, T.
The primary structures and properties of non-stomach lysozymes of sheep and cow, and implication for functional divergence of lysozyme
Eur. J. Biochem.
213
649-658
1993
Bos taurus (P80189), Bos taurus, Ovis aries (P80190), Ovis aries
Manually annotated by BRENDA team
Moss, J.M.; Van Damme, M.P.I.; Murphy, W.H.; Stanton, P.G.; Thomas, P.; Preston, B.N.
Purification, characterization, and biosynthesis of bovine cartilage lysozyme isoforms
Arch. Biochem. Biophys.
339
172-182
1997
Bos taurus
Manually annotated by BRENDA team
Leon-Sicairos, N.; Lopez-Soto, F.; Reyes-Lopez, M.; Godinez-Vargas, D.; Ordaz-Pichardo, C.; de la Garza, M.
Amoebicidal activity of milk, apo-lactoferrin, sIgA and lysozyme
Clin. Med. Res.
4
106-113
2006
Bos taurus, Homo sapiens
Manually annotated by BRENDA team
Nonaka, Y.; Akieda, D.; Aizawa, T.; Watanabe, N.; Kamiya, M.; Kumaki, Y.; Mizuguchi, M.; Kikukawa, T.; Demura, M.; Kawano, K.
X-ray crystallography and structural stability of digestive lysozyme from cow stomach
FEBS J.
276
2192-2200
2009
Bos taurus (Q06283), Bos taurus
Manually annotated by BRENDA team
Barros, G.O.; Ballen, M.A.; Woodard, S.L.; Wilken, L.R.; White, S.G.; Damaj, M.B.; Mirkov, T.E.; Nikolov, Z.L.
Recovery of bovine lysozyme from transgenic sugarcane stalks: extraction, membrane filtration, and purification
Bioprocess Biosyst. Eng.
36
1407-1416
2013
Bos taurus
Manually annotated by BRENDA team