DB code: S00520

RLCP classification	1.30.4950.1 : Hydrolysis
CATH domain	1.10.530.10 : Lysozyme	Catalytic domain
E.C.	3.2.1.17
CSA
M-CSA
MACiE

CATH domain	Related DB codes (homologues)
1.10.530.10 : Lysozyme	D00170 S00509

Uniprot Enzyme Name
UniprotKB	Protein name	Synonyms	CAZy	Pfam
P00718	Lysozyme g	EC 3.2.1.17 1,4-beta-N-acetylmuramidase Goose-type lysozyme	GH23 (Glycoside Hydrolase Family 23)	PF01464 (SLT) [Graphical View]

KEGG enzyme name
lysozyme muramidase globulin G mucopeptide glucohydrolase globulin G1 N,O-diacetylmuramidase lysozyme g L-7001 1,4-N-acetylmuramidase mucopeptide N-acetylmuramoylhydrolase PR1-lysozyme

UniprotKB: Accession Number	Entry name	Activity	Subunit	Subcellular location	Cofactor
P00718	LYG_ANSAN	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.		Secreted.

KEGG Pathways
Map code	Pathways	E.C.

Compound table
	Substrates			Products			Intermediates
KEGG-id	C00889	C00851	C00001	C04394	C00851	C00140
E.C.
Compound	Peptidoglycan	Chitodextrin	H2O	Peptidoglycan(N-acetyl-D-glucosamine)	Chitodextrin	N-Acetyl-D-glucosamine
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
ChEBI			15377 15377	8006 8006		506227 506227
PubChem			22247451 962 22247451 962	5462260 5462260		439174 439174

153lA	Unbound	Unbound		Unbound	Unbound	Unbound
154lA	Unbound	Unbound		Unbound	Bound:NAG-NAG-NAG	Unbound

Reference for Active-site residues
resource	references	E.C.
literature [4]

Active-site residues
PDB	Catalytic residues	Cofactor-binding residues	Modified residues	Main-chain involved in catalysis	Comment

153lA	GLU 73
154lA	GLU 73

References for Catalytic Mechanism
References	Sections	No. of steps in catalysis
[4]	p.64-65
[5]	p.214-218

References
[1]
Resource
Comments
Medline ID
PubMed ID	6866082
Journal	Nature
Year	1983
Volume	303
Pages	828-31
Authors	Grutter MG, Weaver LH, Matthews BW
Title	Goose lysozyme structure: an evolutionary link between hen and bacteriophage lysozymes?
Related PDB
Related UniProtKB
[2]
Resource
Comments
Medline ID
PubMed ID	6442995
Journal	J Mol Evol
Year	1984
Volume	21
Pages	97-111
Authors	Weaver LH, Grutter MG, Remington SJ, Gray TM, Isaacs NW, Matthews BW
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.
Related PDB
Related UniProtKB
[3]
Resource
Comments
Medline ID
PubMed ID	4062692
Journal	Aust J Biol Sci
Year	1985
Volume	38
Pages	13-22
Authors	Isaacs NW, Machin KJ, Masakuni M
Title	Three-dimensional structure of goose-type lysozyme from the egg white of the Australian black swan, Cygnus atratus.
Related PDB
Related UniProtKB
[4]
Resource
Comments	X-ray crystallography
Medline ID
PubMed ID	7823320
Journal	J Mol Biol
Year	1995
Volume	245
Pages	54-68
Authors	Weaver LH, Grutter MG, Matthews BW
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.
Related PDB	153l 154l
Related UniProtKB
[5]
Resource
Comments
Medline ID
PubMed ID	8765301
Journal	EXS
Year	1996
Volume	75
Pages	185-222
Authors	Strynadka NC, James MN
Title	Lysozyme: a model enzyme in protein crystallography.
Related PDB
Related UniProtKB
[6]
Resource
Comments
Medline ID
PubMed ID	8564539
Journal	Nat Struct Biol
Year	1996
Volume	3
Pages	133-40
Authors	Monzingo AF, Marcotte EM, Hart PJ, Robertus JD
Title	Chitinases, chitosanases, and lysozymes can be divided into procaryotic and eucaryotic families sharing a conserved core.
Related PDB
Related UniProtKB
[7]
Resource
Comments
Medline ID
PubMed ID	9774706
Journal	Biochim Biophys Acta
Year	1998
Volume	1388
Pages	53-65
Authors	Honda Y, Fukamizo T
Title	Substrate binding subsites of chitinase from barley seeds and lysozyme from goose egg white.
Related PDB
Related UniProtKB
[8]
Resource
Comments
Medline ID
PubMed ID	12369923
Journal	Curr Protein Pept Sci
Year	2000
Volume	1
Pages	105-24
Authors	Fukamizo T
Title	Chitinolytic enzymes: catalysis, substrate binding, and their application.
Related PDB
Related UniProtKB
[9]
Resource
Comments
Medline ID
PubMed ID	11866097
Journal	Biosci Biotechnol Biochem
Year	2002
Volume	66
Pages	147-56
Authors	Thammasirirak S, Torikata T, Takami K, Murata K, Araki T
Title	The primary structure of cassowary (Casuarius casuarius) goose type lysozyme.
Related PDB
Related UniProtKB

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.

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.

Created	Updated
2004-11-30	2009-02-26