EzCatDB: S00170
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DB codeS00170
CATH domainDomain 12.160.20.10 : Pectate Lyase C-likeCatalytic domain
E.C.4.2.2.10
CSA1idj

CATH domainRelated DB codes (homologues)
2.160.20.10 : Pectate Lyase C-likeS00168,S00171,S00546,S00837,S00169,D00803

Enzyme Name
UniProtKBKEGG

Q01172Q00205
Protein namePectin lyase APectin lyase Bpectin lyase
pectin trans-eliminase
endo-pectin lyase
polymethylgalacturonic transeliminase
pectin methyltranseliminase
pectolyase
PL
PNL
PMGL
SynonymsPLA
EC 4.2.2.10
Pectin lyase II
PLII
PLB
EC 4.2.2.10
PfamPF00544 (Pec_lyase_C)
[Graphical view]
PF00544 (Pec_lyase_C)
[Graphical view]
CAZyPL1 (Polysaccharide Lyase Family)
PL1 (Polysaccharide Lyase Family)


UniProtKB:Accession NumberQ01172Q00205
Entry namePLYA_ASPNGPLYB_ASPNG
ActivityEliminative cleavage of (1->4)-alpha-D- galacturonan methyl ester to give oligosaccharides with 4-deoxy-6- O-methyl-alpha-D-galact-4-enuronosyl groups at their non-reducing ends.Eliminative cleavage of (1->4)-alpha-D- galacturonan methyl ester to give oligosaccharides with 4-deoxy-6- O-methyl-alpha-D-galact-4-enuronosyl groups at their non-reducing ends.
Subunit

Subcellular location

Cofactor


Compound table: links to PDB-related databases & PoSSuM

SubstratesProducts
KEGG-idC00714C00714C04898
CompoundPectinPectinOligosaccharides with terminal 4-deoxy-6-methyl-alpha-D-galact-4-enuronosyl groups
Typecarboxyl group,polysaccharidecarboxyl group,polysaccharidecarbohydrate,polysaccharide
ChEBI


PubChem


           
1idjAUnboundUnboundUnbound
1idjBUnboundUnboundUnbound
1idkAUnboundUnboundUnbound
1qcxAUnboundUnboundUnbound

Active-site residues
resource
Swiss-prot;Q01172, Q00205 & literature [5]
pdbCatalytic residues
         
1idjAARG 176;ARG 236;LYS 239
1idjBARG 176;ARG 236;LYS 239
1idkAARG 176;ARG 236;LYS 239
1qcxAARG 176;ARG 236;LYS 239

References for Catalytic Mechanism
ReferencesSectionsNo. of steps in catalysis
[5]p.333-334

references
[1]
PubMed ID2018526
JournalBiochem Biophys Res Commun
Year1991
Volume176
Pages321-7
AuthorsOhnishi H, Nishida T, Yoshida A, Kamio Y, Izaki K
TitleNucleotide sequence of pnl gene from Erwinia carotovora Er.
[2]
CommentsX-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS).
Medline ID97341230
PubMed ID9195887
JournalStructure
Year1997
Volume5
Pages677-89
AuthorsMayans O, Scott M, Connerton I, Gravesen T, Benen J, Visser J, Pickersgill R, Jenkins J
TitleTwo crystal structures of pectin lyase A from Aspergillus reveal a pH driven conformational change and striking divergence in the substrate-binding clefts of pectin and pectate lyases.
Related PDB1idj,1idk
Related UniProtKBQ01172
[3]
PubMed ID9724625
JournalJ Struct Biol
Year1998
Volume122
Pages236-46
AuthorsJenkins J, Mayans O, Pickersgill R
TitleStructure and evolution of parallel beta-helix proteins.
[4]
CommentsX-ray crystallography
PubMed ID9449837
JournalPlant Physiol
Year1998
Volume116
Pages69-80
AuthorsVitali J, Schick B, Kester HC, Visser J, Jurnak F
TitleThe tree-dimensional structure of aspergillus niger pectin lyase B at 1.7-A resolution.
Related PDB1qcx
[5]
PubMed ID12418964
JournalBiochem J
Year2003
Volume370
Pages331-7
AuthorsSanchez-Torres P, Visser J, Benen JA
TitleIdentification of amino acid residues critical for catalysis and stability in Aspergillus niger family 1 pectin lyase A.


createdupdated
2004-04-042009-02-26
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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)
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