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Literature summary for 3.2.1.17 extracted from

  • 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) (2013), Biosci. Biotechnol. Biochem., 77, 2269-2277.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic analysis Meretrix lusoria

Metals/Ions

Metals/Ions Comment Organism Structure
additional information no increase in activity at high ionic strength Meretrix lusoria

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
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 Meretrix lusoria
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 Meretrix lusoria
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 Meretrix lusoria
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 Meretrix lusoria

Organism

Organism UniProt Comment Textmining
Meretrix lusoria P86383 i-type lysozyme, two isozymes lysozyme A and lysozyme B
-

Purification (Commentary)

Purification (Comment) Organism
native isozymes to homogeneity by ammonium sulfate fractionation, two steps of cation exchange chromatography, and isozyme separation by reversed phase gel filtration Meretrix lusoria

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
620
-
purified lysozyme A, pH 7.0, 25°C Meretrix lusoria
1227
-
purified lysozyme B, pH 7.0, 25°C Meretrix lusoria

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
chitohexaose + H2O
-
Meretrix lusoria ?
-
?
chitopentaose + H2O
-
Meretrix lusoria ?
-
?
lyophilized cell wall of Micrococcus luteus + H2O
-
Meretrix lusoria ?
-
?
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 Meretrix lusoria ?
-
?

Subunits

Subunits Comment Organism
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 Meretrix lusoria
More 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 Meretrix lusoria

Synonyms

Synonyms Comment Organism
i-type lysozyme
-
Meretrix lusoria
lysozyme A
-
Meretrix lusoria
lysozyme B
-
Meretrix lusoria
MLL-A
-
Meretrix lusoria
MLL-B
-
Meretrix lusoria

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
25
-
assay at, lytic activity, substrate lyophilized cell wall of Micrococcus luteus Meretrix lusoria
50
-
assay at, substrate N-acetylglucosamine oligomers Meretrix lusoria

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
5
-
assay at, substrate N-acetylglucosamine oligomers Meretrix lusoria
6.5
-
substrate lyophilized cell wall of Micrococcus luteus, isozyme lysozyme A Meretrix lusoria

General Information

General Information Comment Organism
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 Meretrix lusoria