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Information on EC 4.2.2.2 - pectate lyase

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EC Tree
     4 Lyases
         4.2 Carbon-oxygen lyases
             4.2.2 Acting on polysaccharides
                4.2.2.2 pectate lyase
IUBMB Comments
Favours pectate, the anion, over pectin, the methyl ester (which is the preferred substrate of EC 4.2.2.10, pectin lyase).
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This record set is specific for:
UNIPROT: O68975
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The enzyme appears in viruses and cellular organisms
Synonyms
pectate lyase, polygalacturonate lyase, pectate lyase c, pectate lyase a, alkaline pectate lyase, pectate lyase b, pel-2, alkaline polygalacturonate lyase, pel9a, pel168, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
alpha-1,4-D-endopolygalacturonic acid lyase
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EC 4.2.99.3
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endo-alpha-1,4-polygalacturonic acid lyase
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endogalacturonate transeliminase
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endopectin methyltranseliminase
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lyase, pectate
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pectate transeliminase
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pectic acid lyase
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pectic acid transeliminase
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pectic lyase
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PGA lyase
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Pla
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PLB
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PLC
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poly(1,4-alpha-D-galacturonide) lyase
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polygalacturonate lyase
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polygalacturonic acid lyase
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polygalacturonic transeliminase
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PPase-N
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
elimination
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PATHWAY SOURCE
PATHWAYS
SYSTEMATIC NAME
IUBMB Comments
(1->4)-alpha-D-galacturonan lyase
Favours pectate, the anion, over pectin, the methyl ester (which is the preferred substrate of EC 4.2.2.10, pectin lyase).
CAS REGISTRY NUMBER
COMMENTARY hide
9015-75-2
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
polygalacturonic acid
?
show the reaction diagram
endolytic cleavage
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?
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
ATCC 49397, ATCC 35669 (low activity), and JB580v
SwissProt
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
over 70% of the activity in cell bound fraction
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Manually annotated by BRENDA team
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
O68975_YEREN
601
0
65987
TrEMBL
other Location (Reliability: 5)
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
enzyme from strain ATCC49397 overproduced in Escherichia coli
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Liao, C.H.; Revear, L.; Hotchkiss, A.; Savary, B.
Genetic and biochemical characterization of an exopolygalacturonase and a pectate lyase from Yersinia enterolitica
Can. J. Microbiol.
45
396-403
1999
Yersinia enterocolitica (O68975), Yersinia enterocolitica
Manually annotated by BRENDA team