EzCatDB: S00204
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DB codeS00204
RLCP classification1.32.60200.73 : Hydrolysis
CATH domainDomain 13.20.20.80 : TIM BarrelCatalytic domain
E.C.3.2.1.17,3.2.1.14

CATH domainRelated DB codes (homologues)
3.20.20.80 : TIM BarrelS00202,S00210,S00748,S00906,S00907,S00911,S00912,S00915,M00134,M00160,D00479,S00205,S00206,S00207,S00203,S00208,S00209,S00211,S00213,S00214,M00113,T00307,D00165,D00166,D00169,D00176,D00501,D00502,D00503,D00844,D00861,D00864,M00026,M00112,M00193,M00346,T00057,T00062,T00063,T00066,T00067

Enzyme Name
UniProtKBKEGG

P23472
Protein nameHevamine-Alysozyme
   (EC 3.2.1.17)

muramidase
   (EC 3.2.1.17)

globulin G
   (EC 3.2.1.17)

mucopeptide glucohydrolase
   (EC 3.2.1.17)

globulin G1
   (EC 3.2.1.17)

N,O-diacetylmuramidase
   (EC 3.2.1.17)

lysozyme g
   (EC 3.2.1.17)

L-7001
   (EC 3.2.1.17)

1,4-N-acetylmuramidase
   (EC 3.2.1.17)

mucopeptide N-acetylmuramoylhydrolase
   (EC 3.2.1.17)

PR1-lysozyme
   (EC 3.2.1.17)

chitinase
   (EC 3.2.1.14)

chitodextrinase
   (EC 3.2.1.14)

1,4-beta-poly-N-acetylglucosaminidase
   (EC 3.2.1.14)

poly-beta-glucosaminidase
   (EC 3.2.1.14)

beta-1,4-poly-N-acetyl glucosamidinase
   (EC 3.2.1.14)

poly[1,4-(N-acetyl-beta-D-glucosaminide)] glycanohydrolase
   (EC 3.2.1.14)

SynonymsNone
IncludesChitinase
   EC 3.2.1.14
Lysozyme
   EC 3.2.1.17
PfamPF00704 (Glyco_hydro_18)
[Graphical view]
CAZyGH18 (Glycoside Hydrolase Family)

KEGG pathways
MAP codePathwaysE.C.
MAP00530Aminosugars metabolism3.2.1.14

UniProtKB:Accession NumberP23472
Entry nameCHLY_HEVBR
ActivityRandom hydrolysis of N-acetyl-beta-D- glucosaminide (1->4)-beta-linkages in chitin and chitodextrins.,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
Subcellular locationVacuole. Note=In the lutoids (vacuoles) from rubber latex.
Cofactor

Compound table: links to PDB-related databases & PoSSuM

SubstratesProductsintermediates
KEGG-idC00889C00461C00851C00001C04394C00851C03518C00140
E.C.3.2.1.173.2.1.143.2.1.17,3.2.1.143.2.1.17,3.2.1.143.2.1.173.2.1.173.2.1.143.2.1.17,3.2.1.14
CompoundPeptidoglycanChitinChitodextrinH2OPeptidoglycan(N-acetyl-D-glucosamine)ChitodextrinN-Acetyl-D-glucosaminideN-Acetyl-D-glucosamine
Typeamide group,amine group,peptide/protein,polysaccharideamide group,polysaccharideamide group,polysaccharideH2Oamino acids,amide group,amine group,carbohydrate,lipid,peptide/protein,polysaccharideamide group,polysaccharideamide group,carbohydrateamide group,carbohydrate
ChEBI


15377
8006


506227

PubChem


962
22247451
5462260


439174

                 
1hvmAUnboundUnboundUnbound UnboundUnboundUnboundUnboundUnbound
1hvqAUnboundUnboundUnbound UnboundBound:NAG-NAG-NAGUnboundUnboundUnbound
1lloAUnboundUnboundUnbound UnboundUnboundUnboundUnboundIntermediate-analogue:NAA-NAA-AMI
2hvmAUnboundUnboundUnbound UnboundUnboundUnboundUnboundUnbound

Active-site residues
resource
Swiss-prot
pdbCatalytic residues
         
1hvmAASP 125;GLU 127;TYR 183
1hvqAASP 125;GLU 127;TYR 183
1lloAASP 125;GLU 127;TYR 183
2hvmAASP 125;GLU 127;TYR 183

References for Catalytic Mechanism
ReferencesSectionsNo. of steps in catalysis
[2]Fig.2, Fig.3C, p.15621-15623
[5]Fig.4, p.898-900

references
[1]
CommentsX-ray crystallography (2.2 Angstroms)
Medline ID95219380
PubMed ID7704528
JournalStructure
Year1994
Volume2
Pages1181-89
AuthorsTerwisscha van Scheltinga AC, Kalk KH, Beintema JJ, Dijkstra BW
TitleCrystal structures of hevamine, a plant defence protein with chitinase and lysozyme activity, and its complex with an inhibitor.
Related PDB1hvq
Related UniProtKBP23472
[2]
CommentsX-ray crystallography (1.85 Angstroms)
Medline ID96096984
PubMed ID7495789
JournalBiochemistry
Year1995
Volume34
Pages15619-23
AuthorsTerwisscha van Scheltinga AC, Armand S, Kalk KH, Isogai A, Henrissat B, Dijkstra BW
TitleStereochemistry of chitin hydrolysis by a plant chitinase/lysozyme and X-ray structure of a complex with allosamidin: evidence for substrate assisted catalysis.
Related PDB1llo
Related UniProtKBP23472
[3]
CommentsX-ray crystallography (1.8 Angstroms)
Medline ID96428689
PubMed ID8831791
JournalJ Mol Biol
Year1996
Volume262
Pages243-57
AuthorsTerwisscha van Scheltinga AC, Hennig M, Dijkstra BW
TitleThe 1.8 A resolution structure of hevamine, a plant chitinase/lysozyme, and analysis of the conserved sequence and structure motifs of glycosyl hydrolase family 18.
Related PDB1hvm,2hvm
Related UniProtKBP23472
[4]
CommentsClustering of structures
PubMed ID11742103
JournalProtein Eng
Year2001
Volume14
Pages845-55
AuthorsNagano N, Porter CT, Thornton JM
TitleThe (betaalpha)(8) glycosidases: sequence and structure analyses suggest distant evolutionary relationships.
[5]
CommentsX-ray crystallography of active site mutants
PubMed ID11846790
JournalEur J Biochem
Year2002
Volume269
Pages893-901
AuthorsBokma E, Rozeboom HJ, Sibbald M, Dijkstra BW, Beintema JJ
TitleExpression and characterization of active site mutants of hevamine, a chitinase from the rubber tree Hevea brasiliensis.

comments
This family belongs to glycosidase family-18, which has a retaining mechanism.
According to the literature [2], N-acetyl group of the substrate act as a nucleophile, which will form intramolecular covalent bond within the substrate. Glu127 acts as a general acid or proton donor, which can protonate the O4 atom of the sugar at subsite (+1).
The literature [2] also reported that the conserved residues, Asp125 and Tyr183, interact with the oxygen atom of the oxazoline intermediate. Thus, these residues can function as stabilizers.

createdupdated
2002-11-012009-02-26


Copyright: Nozomi Nagano, JST & CBRC-AIST
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Funded by Grant-in-Aid for Publication of Scientific Research Results/Japan Society for the Promotion of Science (JSPS) (April 2005 - March 2006)
Funded by Grant-in-Aid for Scientific Research (B)/Japan Society for the Promotion of Science (JSPS) (April 2005 - March 2008)
Funded by BIRD/Japan Science and Technology Corporation (JST) (September 2005 - September 2008)
Funded by BIRD/Japan Science and Technology Corporation (JST) (October 2007 - September 2010)
Funded by Grant-in-Aid for Publication of Scientific Research Results/Japan Society for the Promotion of Science (JSPS) (April 2011 - March 2012)
Funded by Grant-in-Aid for Publication of Scientific Research Results/Japan Society for the Promotion of Science (JSPS) (April 2012 - March 2013)
Supported by the commission for the Development of Artificial Gene Synthesis Technology for Creating Innovative Biomaterial from the Ministry of Economy, Trade and Industry (METI) (October 2012 - )
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