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Information on EC 4.2.2.6 - oligogalacturonide lyase

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EC Tree
     4 Lyases
         4.2 Carbon-oxygen lyases
             4.2.2 Acting on polysaccharides
                4.2.2.6 oligogalacturonide lyase
IUBMB Comments
Also catalyses eliminative removal of unsaturated terminal residues from oligosaccharides of D-galacturonate.
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This record set is specific for:
UNIPROT: A1JMA5
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Word Map
The enzyme appears in viruses and cellular organisms
Synonyms
oligogalacturonate lyase, oligogalacturonide lyase, oligogalacturonan lyase, yeogl, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oligogalacturonate lyase
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lyase, oligogalacturonide
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OGTE
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oligogalacturonate lyase
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oligogalacturonide trans-eliminase
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oligogalacturonide transeliminase
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unsaturated oligogalacturonate transeliminase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
4-(4-deoxy-alpha-D-galact-4-enuronosyl)-D-galacturonate = 2 5-dehydro-4-deoxy-D-glucuronate
show the reaction diagram
active site structure modeling and beta-elimination reaction mechanism, overview
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
elimination
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PATHWAY SOURCE
PATHWAYS
SYSTEMATIC NAME
IUBMB Comments
oligogalacturonide lyase
Also catalyses eliminative removal of unsaturated terminal residues from oligosaccharides of D-galacturonate.
CAS REGISTRY NUMBER
COMMENTARY hide
9031-33-8
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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
4-(4-deoxy-alpha-D-gluc-4-enuronosyl)-D-galacturonate
2 5-dehydro-4-deoxy-D-glucuronate
show the reaction diagram
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-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
4-(4-deoxy-alpha-D-gluc-4-enuronosyl)-D-galacturonate
2 5-dehydro-4-deoxy-D-glucuronate
show the reaction diagram
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-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Mn2+
activates, octahedral metal binding site, coordination structure involving N-His287, O-Gln350, N-His353, and His-355, overview
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
pectate
substrate inhibition at high concentrations
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
additional information
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
subsp. enterocolitica, gene ogl, locus YE1876
UniProt
Manually annotated by BRENDA team
subsp. enterocolitica, gene ogl, locus YE1876
UniProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
metabolism
OGL is involved in the pectin degradation pathway performing extracellular pectin depolymerization, overview. In the initial stages, intracellular di- and trigalacturonides are processed into saturated monogalacturonate, GalA, and a 4,5-unsaturated GalA-like monosaccharide, 5-keto-4-deoxyuronate, by the combined activities of an exo-acting family 2 pectate lyase,YePL2B, and oligogalacturonate lyase, YeOGL/YePL22, a lyase family preferentially active on digalacturonides
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
A1JMA5_YERE8
Yersinia enterocolitica serotype O:8 / biotype 1B (strain NCTC 13174 / 8081)
388
0
44211
TrEMBL
other Location (Reliability: 2)
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purified recombinant detagged YeOGL, hanging drop vapor diffusion method, 12.5 mg/ml protein in 20 mM Tris-HCl, precipitation from 0.2 M CaCl2, 0.1 M NaOAc, pH 4.8, 20% PEG 3350, and cryoprotection by 15% ethylene glycol, 18°C, X-ray diffraction structure determination and analysis at 1.65 A resolution
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant N-terminally His-tagged YeOGL from Escherichia coli by nickel affinity chromatography, ultrafiltration, His-tag cleavage through thrombin, and gel filtration
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene ogl, phylogenetic tree of the OGL family, expression of YeOGL containing a thrombin-cleavable N-terminal His6 tag in Escherichia coli BL21-pLysS (DE3) cells
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Abbott, D.W.; Gilbert, H.J.; Boraston, A.B.
The active site of oligogalacturonate lyase provides unique insights into cytoplasmic oligogalacturonate beta-elimination
J. Biol. Chem.
285
39029-39038
2010
Yersinia enterocolitica (A1JMA5), Yersinia enterocolitica, Yersinia enterocolitica 8081 (A1JMA5)
Manually annotated by BRENDA team