Any feedback?
Please rate this page
(enzyme.php)
(0/150)

BRENDA support

BRENDA Home
show all | hide all No of entries

Information on EC 3.2.1.17 - lysozyme and Organism(s) Musca domestica and UniProt Accession Q7YT16

for references in articles please use BRENDA:EC3.2.1.17
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
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.
Specify your search results
Select one or more organisms in this record: ?
This record set is specific for:
Musca domestica
UNIPROT: Q7YT16
Show additional data
Do not include text mining results
Include (text mining) results
Include results (AMENDA + additional results, but less precise)
Word Map
hide
The taxonomic range for the selected organisms is: Musca domestica
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
-
lysozyme 1
precursor
lysozyme 1 precursor
-
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
-
-
-
-
Lys-rich lysozyme 2
-
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
4-methylumbelliferyl-beta-D-N,N',N''-triacetylchitotrioside + H2O
?
show the reaction diagram
-
-
-
-
?
glycol chitin + H2O
chitin oligosaccharides
show the reaction diagram
-
-
-
-
?
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
additional information
?
-
recombinant enzyme displays inhibitory activity against Gram-negative and Gram-positive bacteria
-
-
?
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4
lytic activity towards Micrococcus lysodeikticus
4.7
substrate: N,N',N''-triacetylchitotrioside
additional information
-
the acidic pH optimum for MdL2 and MdL1 activities upon methylumbelliferylchitotrioside is determined by the presence of N46, S106 and T107 in the environment of their catalytic residues, which favors pKas reduction. The acidic pH optimum upon bacterial walls is determined by a low concentration of positive charges on the MdL2 and MdL1 surfaces
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
3.3 - 4.7
pH 3.3: about 70% of maximal activity, pH 4.7: about 50% of maximal activity, substrate: N,N',N''-triacetyl chitotrioside
3.4 - 6.5
pH 3.4: about 40% of maximal activity, pH 6.5: about 40% of maximal activity, lytic activity towards Micrococcus lysodeikticus
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.7
calculated
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
SwissProt
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
from larva
Manually annotated by BRENDA team
high protein expression
Manually annotated by BRENDA team
additional information
low expression at embryo stage. MRNA is upregulated 2 h post bacterial challenge, maintained for 6 h, and slightly declines from 12 to 24 h post-injection
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
comparison of the structure, surface charge, dissociation constants, and pH optimum of the fly enzyme with the enzyme from egg white, overview
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
LYS1_MUSDO
141
0
15733
Swiss-Prot
Secretory Pathway (Reliability: 2)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
13800
x * 13800, calculated
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
x * 13800, calculated
additional information
-
structure analysis of MdL1 and MdL2, overview. Residues S106-T107 delimit a polar pocket around E32, as catalytic acid/base, and N46 contributes to the positioning of D50, as catalytic nucleophile
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
sequence contains eight cysteines within mature peptides forming 4 pairs of disulfide bridges necessary for enzymatic activity
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
sitting-drop vapour-diffusion method in the presence of ammonium sulfate or PEG/2-propanol as the precipitant. X-ray diffraction data are collected to a maximum resolution of 1.9 A using synchrotron radiation. The lysozyme 1 crystals belong to the monoclinic space group P2(1), unit-cell parameters a = 36.52, b = 79.44, c = 45.20 A, beta = 102.97°
vapour-diffusion sitting-drop method, structure of lysozyme c in native form and complexed form with (N-acetylglucosamine)3
purified recombinant MdL2, sitting drop vapour diffusion method, 18°C, precipitant solution containing 28% isopropanol, 21% PEG 4000, and 0.115 M sodium citrate pH 4.2, addition of 0.2 M ammonium acetate, 30% 2-methyl-2,2-pentanediol, 0.1 M sodium citrate, pH 5.6, X-ray diffraction structure determination and analysis at 1.9 A resolution, modeling
-
sitting-drop vapour-diffusion method in the presence of ammonium sulfate or PEG/2-propanol as the precipitant. X-ray diffraction data are collected to a maximum resolution of 1.9 A using synchrotron radiation. The lysozyme 2 crystals belong to the orthorhombic space group P2(1)2(1)2, unit-cell parameters are a = 73.90, b = 96.40, c = 33.27 A
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
N46D/S106V/T107A
-
site-directed mutagenesis of isozyme MdL2, the mutant pKas are increased compared to the wild-type pKas
additional information
-
introduction of six basic residues onMdL1 surface increases by 1 unit the pH optimum for the activity upon bacterial walls
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant wild-type and mutant MdL2s from Pichia pastoris by ammonium sulfate fractionation, and cation exchange, for the sextuple mutant, or anion exchange, for the other mutants, chromatography
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant expression of wild-type and mutant MdL1 and MdL2 in Pichia pastoris
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Ito, Y.; Nakamura, M.; Hotani, T.; Imoto, T.
Insect lysozyme from house fly (Musca domestica) larvae: Possible digestive function based on sequence and enzymatic properties
J. Biochem.
118
546-551
1995
Musca domestica
Manually annotated by BRENDA team
Marana, S.R.; Cancado, F.C.; Valerio, A.A.; Ferreira, C.; Terra, W.R.; Barbosa, J.A.
Crystallization, data collection and phasing of two digestive lysozymes from Musca domestica
Acta Crystallogr. Sect. F
62
750-752
2006
Musca domestica (Q7YT16), Musca domestica (Q7YT17), Musca domestica
Manually annotated by BRENDA team
Cancado, F.C.; Valerio, A.A.; Marana, S.R.; Barbosa, J.A.
The crystal structure of a lysozyme c from housefly Musca domestica, the first structure of a digestive lysozyme
J. Struct. Biol.
160
83-92
2007
Musca domestica (Q7YT16), Musca domestica
Manually annotated by BRENDA team
Ren, Q.; Zhao, X.; Wang, J.
Molecular characterization and expression analysis of a chicken-type lysozyme gene from housefly (Musca domestica)
J. Genet. Genomics
36
7-16
2009
Musca domestica (B3GQR5)
Manually annotated by BRENDA team
Cancado, F.C.; Barbosa, J.A.; Marana, S.R.
Role of the triad N46, S106 and T107 and the surface charges in the determination of the acidic pH optimum of digestive lysozymes from Musca domestica
Comp. Biochem. Physiol. B
155
387-395
2010
Musca domestica
Manually annotated by BRENDA team