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Enzyme Name | UniProtKB | KEGG |
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| P00718 |
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Protein name | Lysozyme g | lysozymemuramidaseglobulin Gmucopeptide glucohydrolaseglobulin G1N,O-diacetylmuramidaselysozyme gL-70011,4-N-acetylmuramidasemucopeptide N-acetylmuramoylhydrolasePR1-lysozyme |
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Synonyms | EC 3.2.1.171,4-beta-N-acetylmuramidaseGoose-type lysozyme |
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Pfam | PF01464 (SLT) [Graphical view]
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CAZy | GH23 (Glycoside Hydrolase Family)
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UniProtKB:Accession Number | P00718 |
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Entry name | LYG_ANSAN |
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Activity | Hydrolysis of (1->4)-beta-linkages between N- acetylmuramic acid and N-acetyl-D-glucosamine residues in a peptidoglycan and between N-acetyl-D-glucosamine residues in chitodextrins. |
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Subunit |
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Subcellular location | Secreted. |
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Cofactor |
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Compound table: links to PDB-related databases & PoSSuM |
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| Substrates | Products |
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KEGG-id | C00889 | C00851 | C00001 | C04394 | C00851 | C00140 |
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Compound | Peptidoglycan | Chitodextrin | H2O | Peptidoglycan(N-acetyl-D-glucosamine) | Chitodextrin | N-Acetyl-D-glucosamine |
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Type | amino acids,amide group,amine group,carbohydrate,peptide/protein,polysaccharide | amide group,polysaccharide | H2O | amino acids,amide group,amine group,carbohydrate,lipid,peptide/protein,polysaccharide | amide group,polysaccharide | amide group,carbohydrate |
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ChEBI |
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| 15377
| 8006
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| 506227
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PubChem |
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| 962 22247451
| 5462260
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| 439174
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153lA |  |  |  |  |  |  |  | Unbound | Unbound | | Unbound | Unbound | Unbound |
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154lA |  |  |  |  |  |  |  | Unbound | Unbound | | Unbound | Bound:NAG-NAG-NAG | Unbound |
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Active-site residues | resource |
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literature [4] | pdb | Catalytic residues |
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153lA |  |  |  |  |  |  |  | GLU 73
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154lA |  |  |  |  |  |  |  | GLU 73
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References for Catalytic Mechanism | References | Sections | No. of steps in catalysis |
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[4] | p.64-65 |
| [5] | p.214-218 |
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references | [1] |
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PubMed ID | 6866082 |
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Journal | Nature |
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Year | 1983 |
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Volume | 303 |
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Pages | 828-31 |
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Authors | Grutter MG, Weaver LH, Matthews BW |
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Title | Goose lysozyme structure: an evolutionary link between hen and bacteriophage lysozymes? |
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[2] |
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PubMed ID | 6442995 |
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Journal | J Mol Evol |
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Year | 1984 |
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Volume | 21 |
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Pages | 97-111 |
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Authors | Weaver LH, Grutter MG, Remington SJ, Gray TM, Isaacs NW, Matthews BW |
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Title | Comparison of goose-type, chicken-type, and phage-type lysozymes illustrates the changes that occur in both amino acid sequence and three-dimensional structure during evolution. |
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[3] |
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PubMed ID | 4062692 |
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Journal | Aust J Biol Sci |
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Year | 1985 |
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Volume | 38 |
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Pages | 13-22 |
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Authors | Isaacs NW, Machin KJ, Masakuni M |
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Title | Three-dimensional structure of goose-type lysozyme from the egg white of the Australian black swan, Cygnus atratus. |
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[4] |
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Comments | X-ray crystallography |
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PubMed ID | 7823320 |
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Journal | J Mol Biol |
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Year | 1995 |
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Volume | 245 |
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Pages | 54-68 |
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Authors | Weaver LH, Grutter MG, Matthews BW |
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Title | The refined structures of goose lysozyme and its complex with a bound trisaccharide show that the "goose-type" lysozymes lack a catalytic aspartate residue. |
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Related PDB | 153l,154l |
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[5] |
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PubMed ID | 8765301 |
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Journal | EXS |
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Year | 1996 |
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Volume | 75 |
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Pages | 185-222 |
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Authors | Strynadka NC, James MN |
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Title | Lysozyme: a model enzyme in protein crystallography. |
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[6] |
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PubMed ID | 8564539 |
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Journal | Nat Struct Biol |
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Year | 1996 |
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Volume | 3 |
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Pages | 133-40 |
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Authors | Monzingo AF, Marcotte EM, Hart PJ, Robertus JD |
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Title | Chitinases, chitosanases, and lysozymes can be divided into procaryotic and eucaryotic families sharing a conserved core. |
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[7] |
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PubMed ID | 9774706 |
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Journal | Biochim Biophys Acta |
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Year | 1998 |
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Volume | 1388 |
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Pages | 53-65 |
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Authors | Honda Y, Fukamizo T |
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Title | Substrate binding subsites of chitinase from barley seeds and lysozyme from goose egg white. |
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[8] |
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PubMed ID | 12369923 |
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Journal | Curr Protein Pept Sci |
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Year | 2000 |
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Volume | 1 |
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Pages | 105-24 |
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Authors | Fukamizo T |
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Title | Chitinolytic enzymes: catalysis, substrate binding, and their application. |
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[9] |
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PubMed ID | 11866097 |
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Journal | Biosci Biotechnol Biochem |
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Year | 2002 |
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Volume | 66 |
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Pages | 147-56 |
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Authors | Thammasirirak S, Torikata T, Takami K, Murata K, Araki T |
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Title | The primary structure of cassowary (Casuarius casuarius) goose type lysozyme. |
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comments | This enzyme belongs to the glycosidase family-23. Although either Asp86 or Asp97 has been annotated as a counterpart to Asp52 of hen egg white lysozyme (S00509 in EzCatDB), the exact position is distant from that of the couterpart, suggesting that the second acidic residue, involved in catalysis, is not important in this enzyme (see [4]). The paper [4] ruled out the possibility of a double displacement mechanism for this enzyme, since the second catalytic residue, acting as the nucleophile, is not essential. Taken together, the catalytic reaction probably proceeds as follows: (1) Glu73 acts as a general acid, to protonates the glycosidic oxygen of the scissile bond, leading to the formation of an oxocarbonium ion intermediate. (2) The sidechain of Glu73 acts as a stabilizer, which stabilizes the oxocarbonium ion intermediate, and also acts as a general base, which activates a nearby water. (3) Finally, the activated water makes a nucleophilic attack on the intermediate to complete the hydrolysis reaction.
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created | updated |
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2004-11-30 | 2009-02-26 |
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