Lysozyme

LYZ
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 133L, 134L, 1B5U, 1B5V, 1B5W, 1B5X, 1B5Y, 1B5Z, 1B7L, 1B7M, 1B7N, 1B7O, 1B7P, 1B7Q, 1B7R, 1B7S, 1BB3, 1BB4, 1BB5, 1C43, 1C45, 1C46, 1C7P, 1CJ6, 1CJ7, 1CJ8, 1CJ9, 1CKC, 1CKD, 1CKF, 1CKG, 1CKH, 1D6P, 1D6Q, 1DI3, 1DI4, 1DI5, 1EQ4, 1EQ5, 1EQE, 1GAY, 1GAZ, 1GB0, 1GB2, 1GB3, 1GB5, 1GB6, 1GB7, 1GB8, 1GB9, 1GBO, 1GBW, 1GBX, 1GBY, 1GBZ, 1GDW, 1GDX, 1GE0, 1GE1, 1GE2, 1GE3, 1GE4, 1GEV, 1GEZ, 1GF0, 1GF3, 1GF4, 1GF5, 1GF6, 1GF7, 1GF8, 1GF9, 1GFA, 1GFE, 1GFG, 1GFH, 1GFJ, 1GFK, 1GFR, 1GFT, 1GFU, 1GFV, 1HNL, 1I1Z, 1I20, 1I22, 1INU, 1IOC, 1IP1, 1IP2, 1IP3, 1IP4, 1IP5, 1IP6, 1IP7, 1IWT, 1IWU, 1IWV, 1IWW, 1IWX, 1IWY, 1IWZ, 1IX0, 1IY3, 1IY4, 1JKA, 1JKB, 1JKC, 1JKD, 1JSF, 1JWR, 1LAA, 1LHH, 1LHI, 1LHJ, 1LHK, 1LHL, 1LHM, 1LMT, 1LOZ, 1LYY, 1LZ1, 1LZ4, 1LZ5, 1LZ6, 1LZR, 1LZS, 1OP9, 1OUA, 1OUB, 1OUC, 1OUD, 1OUE, 1OUF, 1OUG, 1OUH, 1OUI, 1OUJ, 1QSW, 1RE2, 1REM, 1REX, 1REY, 1REZ, 1TAY, 1TBY, 1TCY, 1TDY, 1UBZ, 1W08, 1WQM, 1WQN, 1WQO, 1WQP, 1WQQ, 1WQR, 1YAM, 1YAN, 1YAO, 1YAP, 1YAQ, 207L, 208L, 2BQA, 2BQB, 2BQC, 2BQD, 2BQE, 2BQF, 2BQG, 2BQH, 2BQI, 2BQJ, 2BQK, 2BQL, 2BQM, 2BQN, 2BQO, 2HEA, 2HEB, 2HEC, 2HED, 2HEE, 2HEF, 2LHM, 2MEA, 2MEB, 2MEC, 2MED, 2MEE, 2MEF, 2MEG, 2MEH, 2MEI, 2NWD, 2ZIJ, 2ZIK, 2ZIL, 2ZWB, 3EBA, 3FE0, 3LHM, 3LN2, 4I0C, 4ML7, 4R0P
Identifiers
Aliases	LYZ, LZM, LYZF1, lysozyme
External IDs	OMIM: 153450 MGI: 96902 HomoloGene: 121490 GeneCards: LYZ
Gene ontology Molecular function • catalytic activity • lysozyme activity • hydrolase activity • hydrolase activity, acting on glycosyl bonds • identical protein binding Cellular component • extracellular space • extracellular region • extracellular exosome Biological process • cellular protein metabolic process • metabolic process • retina homeostasis • inflammatory response • cytolysis • defense response to bacterium Sources:Amigo / QuickGO
RNA expression pattern
More reference expression data
Orthologs
Species	Human	Mouse
Entrez	4069	17110
Ensembl	ENSG00000090382	ENSMUSG00000069515
UniProt	P61626	P17897
RefSeq (mRNA)	NM_000239	NM_013590
RefSeq (protein)	NP_000230.1	NP_038618.1
Location (UCSC)	Chr 12: 69.35 – 69.35 Mb	Chr 10: 117.29 – 117.29 Mb
PubMed search	[1]	[2]
Wikidata

Lysozymes, also known as muramidase or N-acetylmuramide glycanhydrolase, are glycoside hydrolases. These are enzymes (EC 3.2.1.17) that damage bacterial cell walls by catalyzing 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. Lysozyme is abundant in a number of secretions, such as tears, saliva, human milk, and mucus. It is also present in cytoplasmic granules of the macrophages and the polymorphonuclear neutrophils (PMNs). Large amounts of lysozyme can be found in egg white. C-type lysozymes are closely related to alpha-lactalbumin in sequence and structure, making them part of the same family. In humans, the lysozyme enzyme is encoded by the LYZ gene.^[3][4]

Function

The enzyme functions by attacking peptidoglycans (found in the cell walls of bacteria, especially Gram-positive bacteria) and hydrolyzing the glycosidic bond that connects N-acetylmuramic acid with the fourth carbon atom of N-acetylglucosamine. It does this by binding to the peptidoglycan molecule in the binding site within the prominent cleft between its two domains. This causes the substrate molecule to adopt a strained conformation similar to that of the transition state.^[5] According to Phillips-Mechanism, the lysozyme binds to a hexasaccharide. The lysozyme then distorts the fourth sugar in hexasaccharide (the D ring) into a half-chair conformation. In this stressed state, the glycosidic bond is easily broken.

Overview of the reaction

The amino acid side-chains glutamic acid 35 (Glu35) and aspartate 52 (Asp52) have been found to be critical to the activity of this enzyme. Glu35 acts as a proton donor to the glycosidic bond, cleaving the C-O bond in the substrate, whereas Asp52 acts as a nucleophile to generate a glycosyl enzyme intermediate. The glycosyl enzyme intermediate then reacts with a water molecule, to give the product of hydrolysis and leaving the enzyme unchanged.^[6]

Mechanism of lysozyme action

Role in disease

Lysozyme is part of the innate immune system. Reduced lysozyme levels have been associated with bronchopulmonary dysplasia in newborns.^[7] Children fed infant formula lacking lysozyme in their diet have three times the rate of diarrheal disease.^[8] Since lysozyme is a natural form of protection from Gram-positive pathogens like Bacillus and Streptococcus,^[9] a deficiency due to infant formula feeding can lead to increased incidence of disease. Whereas the skin is a protective barrier due to its dryness and acidity, the conjunctiva (membrane covering the eye) is, instead, protected by secreted enzymes, mainly lysozyme and defensin. However, when these protective barriers fail, conjunctivitis results.

In certain cancers (especially myelomonocytic leukemia) excessive production of lysozyme by cancer cells can lead to toxic levels of lysozyme in the blood. High lysozyme blood levels can lead to kidney failure and low blood potassium, conditions that may improve or resolve with treatment of the primary malignancy.

Serum lysozyme is much less specific for diagnosis of sarcoidosis than serum Angiotensin Converting Enzyme, since it is more sensitive, it is used as a marker of sarcoidosis disease activity and suitable for disease monitoring in proven cases ^[10]

Hyperglycemia, such as in diabetes, causes lysozyme glycation, which reduces its antimicrobial properties, thus increasing the infection susceptibility in diabetic patients.

History

The antibacterial property of hen egg white, due to the lysozyme it contains, was first observed by Laschtschenko in 1909,^[11] although it was not until 1922 that the name 'lysozyme' was coined, by Alexander Fleming (1881–1955), the discoverer of penicillin.^[12] Fleming first observed the antibacterial action of lysozyme when he treated bacterial cultures with nasal mucus from a patient suffering from a head cold.^[12]

The three-dimensional structure of hen egg white lysozyme was described by David Chilton Phillips (1924–1999) in 1965, when he obtained the first 2-ångström (200 pm) resolution model via X-ray crystallography.^[13][14] The structure was publicly presented at a Royal Institution lecture in 1965.^[15] Lysozyme was the second protein structure and the first enzyme structure to be solved via X-ray diffraction methods, and the first enzyme to be fully sequenced that contains all twenty common amino acids.^[16] As a result of Phillips' elucidation of the structure of lysozyme, it was also the first enzyme to have a detailed, specific mechanism suggested for its method of catalytic action.^[17][18][19] This work led Phillips to provide an explanation for how enzymes speed up a chemical reaction in terms of its physical structures. The original mechanism proposed by Phillips was more recently revised.^[20]

Chemical synthesis

The first chemical synthesis of a lysozyme protein was attempted by Prof. George W. Kenner and his group at the University of Liverpool in England.^[21] This was finally achieved in 2007 by Steve Kent at the University of Chicago who made synthetic functional lysozyme molecule.^[22]

Other applications

Lysozyme crystals have been used to grow other functional materials for catalysis and biomedical applications.^[23][24][25]

See also

• Egg allergy

References

External links

• Muramidase at the US National Library of Medicine Medical Subject Headings (MeSH)
• Proteopedia.org HEW Lysozyme

PDB gallery
133l: ROLE OF ARG 115 IN THE CATALYTIC ACTION OF HUMAN LYSOZYME. X-RAY STRUCTURE OF HIS 115 AND GLU 115 MUTANTS  134l: ROLE OF ARG 115 IN THE CATALYTIC ACTION OF HUMAN LYSOZYME. X-RAY STRUCTURE OF HIS 115 AND GLU 115 MUTANTS  1b5u: CONTRIBUTION OF HYDROGEN BONDS TO THE CONFORMATIONAL STABILITY OF HUMAN LYSOZYME: CALORIMETRY AND X-RAY ANALYSIS OF SIX SER->ALA MUTANT  1b5v: CONTRIBUTION OF HYDROGEN BONDS TO THE CONFORMATIONAL STABILITY OF HUMAN LYSOZYME: CALORIMETRY AND X-RAY ANALYSIS OF SIX SER->ALA MUTANTS  1b5w: CONTRIBUTION OF HYDROGEN BONDS TO THE CONFORMATIONAL STABILITY OF HUMAN LYSOZYME: CALORIMETRY AND X-RAY ANALYSIS OF SIX SER->ALA MUTANTS  1b5x: Contribution of hydrogen bonds to the conformational stability of human lysozyme: calorimetry and x-ray analysis of six ser->ala mutants  1b5y: CONTRIBUTION OF HYDROGEN BONDS TO THE CONFORMATIONAL STABILITY OF HUMAN LYSOZYME: CALORIMETRY AND X-RAY ANALYSIS OF SIX SER->ALA MUTANTS  1b5z: CONTRIBUTION OF HYDROGEN BONDS TO THE CONFORMATIONAL STABILITY OF HUMAN LYSOZYME: CALORIMETRY AND X-RAY ANALYSIS OF SIX SER->ALA MUTANTS  1b7l: VERIFICATION OF SPMP USING MUTANT HUMAN LYSOZYMES  1b7m: VERIFICATION OF SPMP USING MUTANT HUMAN LYSOZYMES  1b7n: VERIFICATION OF SPMP USING MUTANT HUMAN LYSOZYMES  1b7o: VERIFICATION OF SPMP USING MUTANT HUMAN LYSOZYMES  1b7p: VERIFICATION OF SPMP USING MUTANT HUMAN LYSOZYMES  1b7q: VERIFICATION OF SPMP USING MUTANT HUMAN LYSOZYMES  1b7r: VERIFICATION OF SPMP USING MUTANT HUMAN LYSOZYMES  1b7s: VERIFICATION OF SPMP USING MUTANT HUMAN LYSOZYMES  1bb3: HUMAN LYSOZYME MUTANT A96L  1bb4: HUMAN LYSOZYME DOUBLE MUTANT A96L, W109H  1bb5: HUMAN LYSOZYME MUTANT A96L COMPLEXED WITH CHITOTRIOSE  1c43: MUTANT HUMAN LYSOZYME WITH FOREIGN N-TERMINAL RESIDUES  1c45: MUTANT HUMAN LYSOZYME WITH FOREIGN N-TERMINAL RESIDUES  1c46: MUTANT HUMAN LYSOZYME WITH FOREIGN N-TERMINAL RESIDUES  1c7p: CRYSTAL STRUCTURE OF MUTANT HUMAN LYSOZYME WITH FOUR EXTRA RESIDUES (EAEA) AT THE N-TERMINAL  1cj6: T11A MUTANT HUMAN LYSOZYME  1cj7: T11V MUTANT HUMAN LYSOZYME  1cj8: T40A MUTANT HUMAN LYSOZYME  1cj9: T40V MUTANT HUMAN LYSOZYME  1ckc: T43A MUTANT HUMAN LYSOZYME  1ckd: T43V MUTANT HUMAN LYSOZYME  1ckf: T52A MUTANT HUMAN LYSOZYME  1ckg: T52V MUTANT HUMAN LYSOZYME  1ckh: T70V MUTANT HUMAN LYSOZYME  1d6p: HUMAN LYSOZYME L63 MUTANT LABELLED WITH 2',3'-EPOXYPROPYL N,N'-DIACETYLCHITOBIOSE  1d6q: HUMAN LYSOZYME E102 MUTANT LABELLED WITH 2',3'-EPOXYPROPYL GLYCOSIDE OF N-ACETYLLACTOSAMINE  1di3: ROLE OF AMINO ACID RESIDUES AT TURNS IN THE CONFORMATIONAL STABILITY AND FOLDING OF HUMAN LYSOZYME  1di4: ROLE OF AMINO ACID RESIDUES AT TURNS IN THE CONFORMATIONAL STABILITY AND FOLDING OF HUMAN LYSOZYME  1di5: ROLE OF AMINO ACID RESIDUES AT TURNS IN THE CONFORMATIONAL STABILITY AND FOLDING OF HUMAN LYSOZYME  1eq4: CRYSTAL STRUCTURES OF SALT BRIDGE MUTANTS OF HUMAN LYSOZYME  1eq5: CRYSTAL STRUCTURES OF SALT BRIDGE MUTANTS OF HUMAN LYSOZYME  1eqe: CRYSTAL STRUCTURES OF SALT BRIDGE MUTANTS OF HUMAN LYSOZYME  1gay: CRYSTAL STRUCTURE OF MUTANT HUMAN LYSOZYME SUBSTITUTED AT THE SURFACE POSITIONS  1gaz: Crystal Structure of Mutant Human Lysozyme Substituted at the Surface Positions  1gb0: CRYSTAL STRUCTURE OF MUTANT HUMAN LYSOZYME SUBSTITUTED AT THE SURFACE POSITIONS  1gb2: CRYSTAL STRUCTURE OF MUTANT HUMAN LYSOZYME SUBSTITUTED AT THE SURFACE POSITIONS  1gb3: CRYSTAL STRUCTURE OF MUTANT HUMAN LYSOZYME SUBSTITUTED AT THE SURFACE POSITIONS  1gb5: CRYSTAL STRUCTURE OF MUTANT HUMAN LYSOZYME SUBSTITUTED AT THE SURFACE POSITIONS  1gb6: CRYSTAL STRUCTURE OF MUTANT HUMAN LYSOZYME SUBSTITUTED AT THE SURFACE POSITIONS  1gb7: CRYSTAL STRUCTURE OF MUTANT HUMAN LYSOZYME SUBSTITUTED AT THE SURFACE POSITIONS  1gb8: CRYSTAL STRUCTURE OF MUTANT HUMAN LYSOZYME SUBSTITUTED AT THE SURFACE POSITIONS  1gb9: CRYSTAL STRUCTURE OF MUTANT HUMAN LYSOZYME SUBSTITUTED AT THE SURFACE POSITIONS  1gbo: CRYSTAL STRUCTURE OF MUTANT HUMAN LYSOZYME SUBSTITUTED AT THE SURFACE POSITIONS  1gbw: CRYSTAL STRUCTURE OF MUTANT HUMAN LYSOZYME SUBSTITUTED AT THE SURFACE POSITIONS  1gbx: CRYSTAL STRUCTURE OF MUTANT HUMAN LYSOZYME SUBSTITUTED AT THE SURFACE POSITIONS  1gby: CRYSTAL STRUCTURE OF MUTANT HUMAN LYSOZYME SUBSTITUTED AT THE SURFACE POSITIONS  1gbz: CRYSTAL STRUCTURE OF MUTANT HUMAN LYSOZYME SUBSTITUTED AT THE SURFACE POSITIONS  1gdw: CRYSTAL STRUCTURE OF MUTANT HUMAN LYSOZYME SUBSTITUTED AT LEFT-HANDED HELICAL POSITIONS  1gdx: CRYSTAL STRUCTURE OF MUTANT HUMAN LYSOZYME SUBSTITUTED AT LEFT-HANDED HELICAL POSITIONS  1ge0: CRYSTAL STRUCTURE OF MUTANT HUMAN LYSOZYME SUBSTITUTED AT LEFT-HANDED HELICAL POSITIONS  1ge1: CRYSTAL STRUCTURE OF MUTANT HUMAN LYSOZYME SUBSTITUTED AT LEFT-HANDED HELICAL POSITIONS  1ge2: CRYSTAL STRUCTURE OF MUTANT HUMAN LYSOZYME SUBSTITUTED AT LEFT-HANDED HELICAL POSITIONS  1ge3: CRYSTAL STRUCTURE OF MUTANT HUMAN LYSOZYME SUBSTITUTED AT LEFT-HANDED HELICAL POSITIONS  1ge4: CRYSTAL STRUCTURE OF MUTANT HUMAN LYSOZYME SUBSTITUTED AT LEFT-HANDED HELICAL POSITIONS  1gev: BURIED POLAR MUTANT HUMAN LYSOZYME  1gez: BURIED POLAR MUTANT HUMAN LYSOZYME  1gf0: BURIED POLAR MUTANT HUMAN LYSOZYME  1gf3: BURIED POLAR MUTANT HUMAN LYSOZYME  1gf4: BURIED POLAR MUTANT HUMAN LYSOZYME  1gf5: BURIED POLAR MUTANT HUMAN LYSOZYME  1gf6: BURIED POLAR MUTANT HUMAN LYSOZYME  1gf7: BURIED POLAR MUTANT HUMAN LYSOZYME  1gf8: CRYSTAL STRUCTURE OF MUTANT HUMAN LYSOZYME SUBSTITUTED AT THE SURFACE POSITIONS  1gf9: CRYSTAL STRUCTURE OF MUTANT HUMAN LYSOZYME SUBSTITUTED AT THE SURFACE POSITIONS  1gfa: CRYSTAL STRUCTURE OF MUTANT HUMAN LYSOZYME SUBSTITUTED AT THE SURFACE POSITIONS  1gfe: CRYSTAL STRUCTURE OF MUTANT HUMAN LYSOZYME SUBSTITUTED AT THE SURFACE POSITIONS  1gfg: CRYSTAL STRUCTURE OF MUTANT HUMAN LYSOZYME SUBSTITUTED AT THE SURFACE POSITIONS  1gfh: CRYSTAL STRUCTURE OF MUTANT HUMAN LYSOZYME SUBSTITUTED AT THE SURFACE POSITIONS  1gfj: CRYSTAL STRUCTURE OF MUTANT HUMAN LYSOZYME SUBSTITUTED AT THE SURFACE POSITIONS  1gfk: CRYSTAL STRUCTURE OF MUTANT HUMAN LYSOZYME SUBSTITUTED AT THE SURFACE POSITIONS  1gfr: CRYSTAL STRUCTURE OF MUTANT HUMAN LYSOZYME SUBSTITUTED AT THE SURFACE POSITIONS  1gft: CRYSTAL STRUCTURE OF MUTANT HUMAN LYSOZYME SUBSTITUTED AT THE SURFACE POSITIONS  1gfu: CRYSTAL STRUCTURE OF MUTANT HUMAN LYSOZYME SUBSTITUTED AT THE SURFACE POSITIONS  1gfv: CRYSTAL STRUCTURE OF MUTANT HUMAN LYSOZYME SUBSTITUTED AT THE SURFACE POSITIONS  1hnl: CRYSTAL STRUCTURE OF A GLUTATHIONYLATED HUMAN LYSOZYME: A FOLDING INTERMEDIATE MIMIC IN THE FORMATION OF A DISULFIDE BOND  1i1z: MUTANT HUMAN LYSOZYME (Q86D)  1i20: MUTANT HUMAN LYSOZYME (A92D)  1i22: MUTANT HUMAN LYSOZYME (A83K/Q86D/A92D)  1inu: CRYSTAL STRUCTURE OF MUTANT HUMAN LYSOZYME SUBSTITUTED AT THE SURFACE POSITIONS  1ioc: CRYSTAL STRUCTURE OF MUTANT HUMAN LYSOZYME, EAEA-I56T  1ip1: G37A HUMAN LYSOZYME  1ip2: G48A HUMAN LYSOZYME  1ip3: G68A HUMAN LYSOZYME  1ip4: G72A HUMAN LYSOZYME  1ip5: G105A HUMAN LYSOZYME  1ip6: G127A HUMAN LYSOZYME  1ip7: G129A HUMAN LYSOZYME  1iwt: Crystal Structure Analysis of Human lysozyme at 113K.  1iwu: Crystal Structure Analysis of Human lysozyme at 127K.  1iwv: Crystal Structure Analysis of Human lysozyme at 147K.  1iww: Crystal Structure Analysis of Human lysozyme at 152K.  1iwx: Crystal Structure Analysis of Human lysozyme at 161K.  1iwy: Crystal Structure Analysis of Human lysozyme at 170K.  1iwz: Crystal Structure Analysis of Human lysozyme at 178K.  1ix0: I59A-3SS human lysozyme  1iy3: Solution Structure of the Human lysozyme at 4 degree C  1iy4: Solution structure of the human lysozyme at 35 degree C  1jka: HUMAN LYSOZYME MUTANT WITH GLU 35 REPLACED BY ASP  1jkb: HUMAN LYSOZYME MUTANT WITH GLU 35 REPLACED BY ALA  1jkc: HUMAN LYSOZYME MUTANT WITH TRP 109 REPLACED BY PHE  1jkd: HUMAN LYSOZYME MUTANT WITH TRP 109 REPLACED BY ALA  1jsf: FULL-MATRIX LEAST-SQUARES REFINEMENT OF HUMAN LYSOZYME  1jwr: Crystal structure of human lysozyme at 100 K  1laa: X-RAY STRUCTURE OF GLU 53 HUMAN LYSOZYME  1lhh: ROLE OF PROLINE RESIDUES IN HUMAN LYSOZYME STABILITY: A SCANNING CALORIMETRIC STUDY COMBINED WITH X-RAY STRUCTURE ANALYSIS OF PROLINE MUTANTS  1lhi: ROLE OF PROLINE RESIDUES IN HUMAN LYSOZYME STABILITY: A SCANNING CALORIMETRIC STUDY COMBINED WITH X-RAY STRUCTURE ANALYSIS OF PROLINE MUTANTS  1lhj: ROLE OF PROLINE RESIDUES IN HUMAN LYSOZYME STABILITY: A SCANNING CALORIMETRIC STUDY COMBINED WITH X-RAY STRUCTURE ANALYSIS OF PROLINE MUTANTS  1lhk: ROLE OF PROLINE RESIDUES IN HUMAN LYSOZYME STABILITY: A SCANNING CALORIMETRIC STUDY COMBINED WITH X-RAY STRUCTURE ANALYSIS OF PROLINE MUTANTS  1lhl: ROLE OF PROLINE RESIDUES IN HUMAN LYSOZYME STABILITY: A SCANNING CALORIMETRIC STUDY COMBINED WITH X-RAY STRUCTURE ANALYSIS OF PROLINE MUTANTS  1lhm: THE CRYSTAL STRUCTURE OF A MUTANT LYSOZYME C77(SLASH)95A WITH INCREASED SECRETION EFFICIENCY IN YEAST  1lmt: STRUCTURE OF A CONFORMATIONALLY CONSTRAINED ARG-GLY-ASP SEQUENCE INSERTED INTO HUMAN LYSOZYME  1loz: AMYLOIDOGENIC VARIANT (I56T) VARIANT OF HUMAN LYSOZYME  1lyy: AMYLOIDOGENIC VARIANT (ASP67HIS) OF HUMAN LYSOZYME  1lz1: REFINEMENT OF HUMAN LYSOZYME AT 1.5 ANGSTROMS RESOLUTION. ANALYSIS OF NON-BONDED AND HYDROGEN-BOND INTERACTIONS  1lz4: ENTHALPIC DESTABILIZATION OF A MUTANT HUMAN LYSOZYME LACKING A DISULFIDE BRIDGE BETWEEN CYSTEINE-77 AND CYSTEINE-95  1lz5: STRUCTURAL AND FUNCTIONAL ANALYSES OF THE ARG-GLY-ASP SEQUENCE INTRODUCED INTO HUMAN LYSOZYME  1lz6: STRUCTURAL AND FUNCTIONAL ANALYSES OF THE ARG-GLY-ASP SEQUENCE INTRODUCED INTO HUMAN LYSOZYME  1lzr: STRUCTURAL CHANGES OF THE ACTIVE SITE CLEFT AND DIFFERENT SACCHARIDE BINDING MODES IN HUMAN LYSOZYME CO-CRYSTALLIZED WITH HEXA-N-ACETYL-CHITOHEXAOSE AT PH 4.0  1lzs: STRUCTURAL CHANGES OF THE ACTIVE SITE CLEFT AND DIFFERENT SACCHARIDE BINDING MODES IN HUMAN LYSOZYME CO-CRYSTALLIZED WITH HEXA-N-ACETYL-CHITOHEXAOSE AT PH 4.0  1op9: Complex of human lysozyme with camelid VHH HL6 antibody fragment  1oua: CONTRIBUTION OF HYDROPHOBIC RESIDUES TO THE STABILITY OF HUMAN LYSOZYME: X-RAY STRUCTURE OF THE I56T MUTANT  1oub: CONTRIBUTION OF HYDROPHOBIC RESIDUES TO THE STABILITY OF HUMAN LYSOZYME: X-RAY STRUCTURE OF THE V100A MUTANT  1ouc: CONTRIBUTION OF HYDROPHOBIC RESIDUES TO THE STABILITY OF HUMAN LYSOZYME: X-RAY STRUCTURE OF THE V110A MUTANT  1oud: CONTRIBUTION OF HYDROPHOBIC RESIDUES TO THE STABILITY OF HUMAN LYSOZYME: X-RAY STRUCTURE OF THE V121A MUTANT  1oue: CONTRIBUTION OF HYDROPHOBIC RESIDUES TO THE STABILITY OF HUMAN LYSOZYME: X-RAY STRUCTURE OF THE V125A MUTANT  1ouf: CONTRIBUTION OF HYDROPHOBIC RESIDUES TO THE STABILITY OF HUMAN LYSOZYME: X-RAY STRUCTURE OF THE V130A MUTANT  1oug: CONTRIBUTION OF HYDROPHOBIC RESIDUES TO THE STABILITY OF HUMAN LYSOZYME: X-RAY STRUCTURE OF THE V2A MUTANT  1ouh: CONTRIBUTION OF HYDROPHOBIC RESIDUES TO THE STABILITY OF HUMAN LYSOZYME: X-RAY STRUCTURE OF THE V74A MUTANT  1oui: CONTRIBUTION OF HYDROPHOBIC RESIDUES TO THE STABILITY OF HUMAN LYSOZYME: X-RAY STRUCTURE OF THE V93A MUTANT  1ouj: CONTRIBUTION OF HYDROPHOBIC RESIDUES TO THE STABILITY OF HUMAN LYSOZYME: X-RAY STRUCTURE OF THE V99A MUTANT  1qsw: CRYSTAL STRUCTURE ANALYSIS OF A HUMAN LYSOZYME MUTANT W64C C65A  1re2: HUMAN LYSOZYME LABELLED WITH TWO 2',3'-EPOXYPROPYL BETA-GLYCOSIDE OF N-ACETYLLACTOSAMINE  1rem: HUMAN LYSOZYME WITH MAN-B1,4-GLCNAC COVALENTLY ATTACHED TO ASP53  1rex: NATIVE HUMAN LYSOZYME  1rey: HUMAN LYSOZYME-N,N'-DIACETYLCHITOBIOSE COMPLEX  1rez: HUMAN LYSOZYME-N-ACETYLLACTOSAMINE COMPLEX  1tay: DISSECTION OF THE FUNCTIONAL ROLE OF STRUCTURAL ELEMENTS OF TYROSINE-63 IN THE CATALYTIC ACTION OF HUMAN LYSOZYME  1tby: DISSECTION OF THE FUNCTIONAL ROLE OF STRUCTURAL ELEMENTS OF TYROSINE-63 IN THE CATALYTIC ACTION OF HUMAN LYSOZYME  1tcy: DISSECTION OF THE FUNCTIONAL ROLE OF STRUCTURAL ELEMENTS OF TYROSINE-63 IN THE CATALYTIC ACTION OF HUMAN LYSOZYME  1tdy: DISSECTION OF THE FUNCTIONAL ROLE OF STRUCTURAL ELEMENTS OF TYROSINE-63 IN THE CATALYTIC ACTION OF HUMAN LYSOZYME  1ubz: Crystal structure of Glu102-mutant human lysozyme doubly labeled with 2',3'-epoxypropyl beta-glycoside of N-acetyllactosamine  1w08: STRUCTURE OF T70N HUMAN LYSOZYME  1wqm: CONTRIBUTION OF HYDROGEN BONDS TO THE CONFORMATIONAL STABILITY OF HUMAN LYSOZYME  1wqn: CONTRIBUTION OF HYDROGEN BONDS TO THE CONFORMATIONAL STABILITY OF HUMAN LYSOZYME  1wqo: CONTRIBUTION OF HYDROGEN BONDS TO THE CONFORMATIONAL STABILITY OF HUMAN LYSOZYME  1wqp: CONTRIBUTION OF HYDROGEN BONDS TO THE CONFORMATIONAL STABILITY OF HUMAN LYSOZYME  1wqq: CONTRIBUTION OF HYDROGEN BONDS TO THE CONFORMATIONAL STABILITY OF HUMAN LYSOZYME  1wqr: CONTRIBUTION OF HYDROGEN BONDS TO THE CONFORMATIONAL STABILITY OF HUMAN LYSOZYME  1yam: CONTRIBUTION OF HYDROPHOBIC RESIDUES TO THE STABILITY OF HUMAN LYSOZYME: CALORIMETRIC STUDIES AND X-RAY STRUCTURAL ANALYSIS OF THE FIVE ISOLEUCINE TO VALINE MUTANTS  1yan: CONTRIBUTION OF HYDROPHOBIC RESIDUES TO THE STABILITY OF HUMAN LYSOZYME: CALORIMETRIC STUDIES AND X-RAY STRUCTURAL ANALYSIS OF THE FIVE ISOLEUCINE TO VALINE MUTANTS  1yao: CONTRIBUTION OF HYDROPHOBIC RESIDUES TO THE STABILITY OF HUMAN LYSOZYME: CALORIMETRIC STUDIES AND X-RAY STRUCTURAL ANALYSIS OF THE FIVE ISOLEUCINE TO VALINE MUTANTS  1yap: CONTRIBUTION OF HYDROPHOBIC RESIDUES TO THE STABILITY OF HUMAN LYSOZYME: CALORIMETRIC STUDIES AND X-RAY STRUCTURAL ANALYSIS OF THE FIVE ISOLEUCINE TO VALINE MUTANTS  1yaq: CONTRIBUTION OF HYDROPHOBIC RESIDUES TO THE STABILITY OF HUMAN LYSOZYME: CALORIMETRIC STUDIES AND X-RAY STRUCTURAL ANALYSIS OF THE FIVE ISOLEUCINE TO VALINE MUTANTS  207l: MUTANT HUMAN LYSOZYME C77A  208l: MUTANT HUMAN LYSOZYME C77A  2bqa: CONTRIBUTION OF HYDROPHOBIC EFFECT TO THE CONFORMATIONAL STABILITY OF HUMAN LYSOZYME  2bqb: CONTRIBUTION OF HYDROPHOBIC EFFECT TO THE CONFORMATIONAL STABILITY OF HUMAN LYSOZYME  2bqc: CONTRIBUTION OF HYDROPHOBIC EFFECT TO THE CONFORMATIONAL STABILITY OF HUMAN LYSOZYME  2bqd: CONTRIBUTION OF HYDROPHOBIC EFFECT TO THE CONFORMATIONAL STABILITY OF HUMAN LYSOZYME  2bqe: CONTRIBUTION OF HYDROPHOBIC EFFECT TO THE CONFORMATIONAL STABILITY OF HUMAN LYSOZYME  2bqf: CONTRIBUTION OF HYDROPHOBIC EFFECT TO THE CONFORMATIONAL STABILITY OF HUMAN LYSOZYME  2bqg: CONTRIBUTION OF HYDROPHOBIC EFFECT TO THE CONFORMATIONAL STABILITY OF HUMAN LYSOZYME  2bqh: CONTRIBUTION OF HYDROPHOBIC EFFECT TO THE CONFORMATIONAL STABILITY OF HUMAN LYSOZYME  2bqi: CONTRIBUTION OF HYDROPHOBIC EFFECT TO THE CONFORMATIONAL STABILITY OF HUMAN LYSOZYME  2bqj: CONTRIBUTION OF HYDROPHOBIC EFFECT TO THE CONFORMATIONAL STABILITY OF HUMAN LYSOZYME  2bqk: CONTRIBUTION OF HYDROPHOBIC EFFECT TO THE CONFORMATIONAL STABILITY OF HUMAN LYSOZYME  2bql: CONTRIBUTION OF HYDROPHOBIC EFFECT TO THE CONFORMATIONAL STABILITY OF HUMAN LYSOZYME  2bqm: CONTRIBUTION OF HYDROPHOBIC EFFECT TO THE CONFORMATIONAL STABILITY OF HUMAN LYSOZYME  2bqn: CONTRIBUTION OF HYDROPHOBIC EFFECT TO THE CONFORMATIONAL STABILITY OF HUMAN LYSOZYME  2bqo: CONTRIBUTION OF HYDROPHOBIC EFFECT TO THE CONFORMATIONAL STABILITY OF HUMAN LYSOZYME  2hea: CONTRIBUTION OF WATER MOLECULES IN THE INTERIOR OF A PROTEIN TO THE CONFORMATIONAL STABILITY  2heb: CONTRIBUTION OF WATER MOLECULES IN THE INTERIOR OF A PROTEIN TO THE CONFORMATIONAL STABILITY  2hec: CONTRIBUTION OF WATER MOLECULES IN THE INTERIOR OF A PROTEIN TO THE CONFORMATIONAL STABILITY  2hed: CONTRIBUTION OF WATER MOLECULES IN THE INTERIOR OF A PROTEIN TO THE CONFORMATIONAL STABILITY  2hee: CONTRIBUTION OF WATER MOLECULES IN THE INTERIOR OF A PROTEIN TO THE CONFORMATIONAL STABILITY  2hef: CONTRIBUTION OF WATER MOLECULES IN THE INTERIOR OF A PROTEIN TO THE CONFORMATIONAL STABILITY  2lhm: CRYSTAL STRUCTURES OF THE APO-AND HOLOMUTANT HUMAN LYSOZYMES WITH AN INTRODUCED CA2+ BINDING SITE  2mea: CHANGES IN CONFORMATIONAL STABILITY OF A SERIES OF MUTANT HUMAN LYSOZYMES AT CONSTANT POSITIONS  2meb: CHANGES IN CONFORMATIONAL STABILITY OF A SERIES OF MUTANT HUMAN LYSOZYMES AT CONSTANT POSITIONS  2mec: CHANGES IN CONFORMATIONAL STABILITY OF A SERIES OF MUTANT HUMAN LYSOZYMES AT CONSTANT POSITIONS  2med: CONTRIBUTION OF HYDROPHOBIC EFFECT TO THE CONFORMATIONAL STABILITY OF HUMAN LYSOZYME  2mee: CONTRIBUTION OF HYDROPHOBIC EFFECT TO THE CONFORMATIONAL STABILITY OF HUMAN LYSOZYME  2mef: CONTRIBUTION OF HYDROPHOBIC EFFECT TO THE CONFORMATIONAL STABILITY OF HUMAN LYSOZYME  2meg: CHANGES IN CONFORMATIONAL STABILITY OF A SERIES OF MUTANT HUMAN LYSOZYMES AT CONSTANT POSITIONS.  2meh: CONTRIBUTION OF HYDROPHOBIC EFFECT TO THE CONFORMATIONAL STABILITY OF HUMAN LYSOZYME  2mei: CONTRIBUTION OF HYDROPHOBIC EFFECT TO THE CONFORMATIONAL STABILITY OF HUMAN LYSOZYME  2nwd: Structure of chemically synthesized human lysozyme at 1 Angstrom resolution  3lhm: CRYSTAL STRUCTURES OF THE APO-AND HOLOMUTANT HUMAN LYSOZYMES WITH AN INTRODUCED CA2+ BINDING SITE