Reviewed, UniProtKB/Swiss-Prot P00698 (LYSC_CHICK)

Names and origin

Protein names

Recommended name:
    Lysozyme C
    EC=3.2.1.17
Alternative name(s):
    1,4-beta-N-acetylmuramidase C
    Allergen Gal d IV
    Allergen=Gal d 4

Gene names

Name:

LYZ

Organism

Gallus gallus (Chicken)

Taxonomic identifier

9031 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Archosauria › Dinosauria › Saurischia › Theropoda › Coelurosauria › Aves › Neognathae › Galliformes › Phasianidae › Phasianinae › Gallus

Protein attributes

Sequence length	147 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Lysozymes have primarily a bacteriolytic function; those in tissues and body fluids are associated with the monocyte-macrophage system and enhance the activity of immunoagents.
Catalytic 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.
Subunit structure	Monomer.
Tissue specificity	In the egg white and polymorphonuclear Leukocytes.
Allergenic properties	Causes an allergic reaction in human.
Miscellaneous	Lysozyme C is capable of both hydrolysis and transglycosylation; it shows also a slight esterase activity. It acts rapidly on both peptide-substituted and unsubstituted peptidoglycan, and slowly on chitin oligosaccharides.
Sequence similarities	Belongs to the glycosyl hydrolase 22 family.

Ontologies

Keywords
Disease	Allergen
Domain	Signal
Molecular function	Antimicrobial Bacteriolytic enzyme Glycosidase Hydrolase
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
None. [Check GOA]

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Molecule processing

Signal peptide

1 – 18

18

Chain

19 – 147

129

Lysozyme C

Sites

Active site

53

1

Active site

70

1

Binding site

119

1

Substrate

Amino acid modifications

Disulfide bond

24 ↔ 145

Disulfide bond

48 ↔ 133

Disulfide bond

82 ↔ 98

Disulfide bond

94 ↔ 112

Experimental info

Sequence conflict

49

1

A → V in CAA23711. Ref.1

Sequence conflict

121

1

N → D AA sequence Ref.4

Sequence conflict

124

1

N → S in CAA23711. Ref.1

Sequence conflict

132

1

R → S in AAA48944. Ref.5

Secondary structure

1

.

.

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.

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147

Helix Strand Turn

Details...

Helix

23 – 32

10

Helix

43 – 54

12

Beta strand

61 – 63

3

Beta strand

69 – 71

3

Turn

72 – 75

4

Turn

78 – 80

3

Helix

98 – 102

5

Beta strand

103 – 105

3

Helix

107 – 117

11

Beta strand

119 – 121

3

Helix

122 – 125

4

Helix

127 – 132

6

Turn

133 – 135

3

Helix

138 – 141

4

Turn

142 – 144

3

Sequences

	Sequence		Length	Mass (Da)
	P00698-1 [UniParc]. Last modified July 21, 1986. Version 1. Checksum: 81E85743FF579468	FASTA	147	16,239
	10 20 30 40 50 60 MRSLLILVLC FLPLAALGKV FGRCELAAAM KRHGLDNYRG YSLGNWVCAA KFESNFNTQA 70 80 90 100 110 120 TNRNTDGSTD YGILQINSRW WCNDGRTPGS RNLCNIPCSA LLSSDITASV NCAKKIVSDG 130 140 NGMNAWVAWR NRCKGTDVQA WIRGCRL

References

[1]	"Exons encode functional and structural units of chicken lysozyme." Jung A., Sippel A.E., Grez M., Schutz G. Proc. Natl. Acad. Sci. U.S.A. 77:5759-5763(1980) [PubMed: 6934509] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], SEQUENCE REVISION TO 121.
[2]	"The chicken lysozyme chromatin domain contains a second, widely expressed gene." Chong S., Riggs A.D., Bonifer C. Nucleic Acids Res. 30:463-467(2002) [PubMed: 11788708] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]	"Precursor of egg white lysozyme. Amino acid sequence of an NH2-terminal extension." Palmiter R.D., Gagnon J., Ericsson L.H., Walsh K.A. J. Biol. Chem. 252:6386-6393(1977) [PubMed: 893412] [Abstract] Cited for: PROTEIN SEQUENCE OF 1-20.
[4]	"The amino acid sequence of egg white lysozyme." Canfield R.E. J. Biol. Chem. 238:2698-2707(1963) [PubMed: 14063294] [Abstract] Cited for: PROTEIN SEQUENCE OF 19-147.
[5]	"Isolation of recombinant plasmids bearing cDNA to hen ovomucoid and lysozyme mRNAs." Buell G.N., Wickens M.P., Carbon J., Schimke R.T. J. Biol. Chem. 254:9277-9283(1979) [PubMed: 383714] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 123-146.
[6]	"The disulfide bonds of egg white lysozyme (muramidase)." Canfield R.E., Liu A.K. J. Biol. Chem. 240:1997-2002(1965) [PubMed: 14301784] [Abstract] Cited for: DISULFIDE BONDS.
[7]	"The disulfide bridges of hen's egg-white lysozyme." Jauregui-Adell J., Jolles J., Jolles P. Biochim. Biophys. Acta 107:97-111(1965) [PubMed: 5857373] [Abstract] Cited for: DISULFIDE BONDS.
[8]	"Vertebrate lysozymes." Imoto T., Johnson L.N., North A.C.T., Phillips D.C., Rupley J.A. (In) Boyer P.D. (eds.); The enzymes (3rd ed.), pp.7:665-868, Academic Press, New York (1972) Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS), REVIEW.
[9]	"Structure of hen egg-white lysozyme. A three-dimensional Fourier synthesis at 2-A resolution." Blake C.C.F., Koenig D.F., Mair G.A., North A.C.T., Phillips D.C., Sarma V.R. Nature 206:757-761(1965) [PubMed: 5891407] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
[10]	"The structure of triclinic lysozyme at 2.5-A resolution." Moult J., Yonath A., Traub W., Smilansky A., Podjarny A., Rabinovich D., Saya A. J. Mol. Biol. 100:179-195(1976) [PubMed: 1255711] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF TRICLINIC LYSOZYME.
[11]	"Structures of triclinic mono- and di-N-acetylglucosamine: lysozyme complexes -- a crystallographic study." Kurachi K., Sieker L.C., Jensen L.H. J. Mol. Biol. 101:11-24(1976) [PubMed: 1255720] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF TRICLINIC LYSOZYME.
[12]	"Crystallographic refinement of the three-dimensional structure of the FabD1.3-lysozyme complex at 2.5-A resolution." Fischmann T.O., Bentley G.A., Bhat T.N., Boulot G., Mariuzza R.A., Phillips S.E., Tello D., Poljak R.J. J. Biol. Chem. 266:12915-12920(1991) [PubMed: 1712773] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF COMPLEX WITH ANTIBODY.
[13]	"Sequential 1H NMR assignments and secondary structure of hen egg white lysozyme in solution." Redfield C., Dobson C.M. Biochemistry 27:122-136(1988) [PubMed: 3349024] [Abstract] Cited for: STRUCTURE BY NMR.
[14]	"Structural and dynamical properties of a denatured protein. Heteronuclear 3D NMR experiments and theoretical simulations of lysozyme in 8 M urea." Schwalbe H., Fiebig K.M., Buck M., Jones J.A., Grimshaw S.B., Spencer A., Glaser S.J., Smith L.J., Dobson C.M. Biochemistry 36:8977-8991(1997) [PubMed: 9220986] [Abstract] Cited for: STRUCTURE BY NMR.
[15]	"Conversion of Trp 62 of hen egg-white lysozyme to Tyr by site-directed mutagenesis." Kumagai I., Kojima S., Tamaki E., Miura K. J. Biochem. 102:733-740(1987) [PubMed: 3325501] [Abstract] Cited for: MUTAGENESIS.
+	Additional computationally mapped references.

Web resources

Worthington enzyme manual

Cross-references

Sequence databases

EMBLGenBankDDBJ

J00885 Genomic DNA. Translation: AAA48943.1.
V00428 mRNA. Translation: CAA23711.1.
AF410481 Genomic DNA. Translation: AAL69327.1.
M10640 mRNA. Translation: AAA48944.1.

PIR

LZCH. A93859.

RefSeq

NP_990612.1.

UniGene

Gga.713

3D structure databases

PDBMSD

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
132L	X-ray	1.80	A	20-147	[»]
193L	X-ray	1.33	A	19-147	[»]
194L	X-ray	1.40	A	19-147	[»]
1A2Y	X-ray	1.50	C	19-147	[»]
1AKI	X-ray	1.50	A	19-147	[»]
1AT5	X-ray	1.80	A	19-147	[»]
1AT6	X-ray	1.80	A	19-147	[»]
1AZF	X-ray	1.80	A	19-147	[»]
1B0D	X-ray	1.84	A	19-147	[»]
1B2K	X-ray	1.60	A/B	19-147	[»]
1BGI	X-ray	1.70	A	19-147	[»]
1BHZ	X-ray	3.90	A	19-147	[»]
1BVK	X-ray	2.70	C/F	19-147	[»]
1BVX	X-ray	1.80	A	19-147	[»]
1BWH	X-ray	1.80	A	19-147	[»]
1BWI	X-ray	1.80	A	19-147	[»]
1BWJ	X-ray	1.80	A	19-147	[»]
1C08	X-ray	2.30	C	19-147	[»]
1C10	X-ray	2.03	A	19-147	[»]
1DPW	X-ray	1.64	A	19-147	[»]
1DPX	X-ray	1.65	A	19-147	[»]
1DQJ	X-ray	2.00	C	19-147	[»]
1E8L	NMR	-	A	19-147	[»]
1F0W	X-ray	1.90	A	19-147	[»]
1F10	X-ray	1.70	A	19-147	[»]
1F3J	X-ray	3.10	P/Q	29-42	[»]
1FDL	X-ray	2.50	Y	19-147	[»]
1FLQ	X-ray	1.80	A	19-147	[»]
1FLU	X-ray	1.78	A	19-147	[»]
1FLW	X-ray	1.81	A	19-147	[»]
1FLY	X-ray	1.83	A	19-147	[»]
1FN5	X-ray	1.78	A	19-147	[»]
1G7H	X-ray	1.85	C	19-147	[»]
1G7I	X-ray	1.80	C	19-147	[»]
1G7J	X-ray	1.75	C	19-147	[»]
1G7L	X-ray	2.00	C	19-147	[»]
1G7M	X-ray	1.90	C	19-147	[»]
1GPQ	X-ray	1.60	C/D	19-147	[»]
1GWD	X-ray	1.77	A	19-147	[»]
1GXV	NMR	-	2	19-147	[»]
1GXX	NMR	-	A	19-147	[»]
1H6M	X-ray	1.64	A	19-147	[»]
1H87	X-ray	1.72	A	19-147	[»]
1HC0	X-ray	1.82	A	19-147	[»]
1HEL	X-ray	1.70	A	19-147	[»]
1HEM	X-ray	1.80	A	19-147	[»]
1HEN	X-ray	1.80	A	19-147	[»]
1HEO	X-ray	1.80	A	19-147	[»]
1HEP	X-ray	1.80	A	19-147	[»]
1HEQ	X-ray	1.80	A	19-147	[»]
1HER	X-ray	1.80	A	19-147	[»]
1HEW	X-ray	1.75	A	19-147	[»]
1HF4	X-ray	1.45	A/B	19-147	[»]
1HSW	X-ray	2.00	A	19-147	[»]
1HSX	X-ray	1.90	A	19-147	[»]
1IC4	X-ray	2.50	Y	19-147	[»]
1IC5	X-ray	2.30	Y	19-147	[»]
1IC7	X-ray	2.10	Y	19-147	[»]
1IEE	X-ray	0.94	A	19-147	[»]
1IO5	neutron diffraction	2.00	A	19-147	[»]
1IOQ	X-ray	1.79	A	19-147	[»]
1IOR	X-ray	1.76	A	19-147	[»]
1IOS	X-ray	1.76	A	19-147	[»]
1IOT	X-ray	1.75	A	19-147	[»]
1IR7	X-ray	1.90	A	19-147	[»]
1IR8	X-ray	1.63	A	19-147	[»]
1IR9	X-ray	1.90	A	19-147	[»]
1J1O	X-ray	1.80	Y	19-147	[»]
1J1P	X-ray	1.80	Y	19-147	[»]
1J1X	X-ray	1.80	Y	19-147	[»]
1JA2	X-ray	2.87	A	19-147	[»]
1JA4	X-ray	2.94	A	19-147	[»]
1JA6	X-ray	2.96	A	19-147	[»]
1JA7	X-ray	2.98	A	19-147	[»]
1JIS	X-ray	1.90	A	19-147	[»]
1JIT	X-ray	1.90	A	19-147	[»]
1JIY	X-ray	1.90	A	19-147	[»]
1JJ0	X-ray	1.90	A	19-147	[»]
1JJ1	X-ray	1.90	A	19-147	[»]
1JJ3	X-ray	1.90	A/B	19-147	[»]
1JPO	X-ray	2.10	A	19-147	[»]
1JTO	X-ray	2.50	L/M	19-147	[»]
1JTT	X-ray	2.10	L	19-147	[»]
1KIP	X-ray	2.10	C	19-147	[»]
1KIQ	X-ray	1.85	C	19-147	[»]
1KIR	X-ray	2.00	C	19-147	[»]
1KXW	X-ray	1.96	A	19-147	[»]
1KXX	X-ray	1.71	A	19-147	[»]
1KXY	X-ray	1.79	A	19-147	[»]
1LCN	X-ray	1.63	A/B	19-147	[»]
1LJ3	X-ray	2.00	A/B	19-147	[»]
1LJ4	X-ray	1.95	A/B	19-147	[»]
1LJE	X-ray	2.00	A/B	19-147	[»]
1LJF	X-ray	1.80	A/B	19-147	[»]
1LJG	X-ray	1.90	A/B	19-147	[»]
1LJH	X-ray	1.80	A/B	19-147	[»]
1LJI	X-ray	2.00	A/B	19-147	[»]
1LJJ	X-ray	2.00	A/B	19-147	[»]
1LJK	X-ray	2.10	A/B	19-147	[»]
1LKR	X-ray	1.60	A/B	19-147	[»]