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Information on EC 4.2.1.82 - xylonate dehydratase and Organism(s) Escherichia coli and UniProt Accession P39358

for references in articles please use BRENDA:EC4.2.1.82
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EC Tree
     4 Lyases
         4.2 Carbon-oxygen lyases
             4.2.1 Hydro-lyases
                4.2.1.82 xylonate dehydratase
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This record set is specific for:
Escherichia coli
UNIPROT: P39358 not found.
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Word Map
The taxonomic range for the selected organisms is: Escherichia coli
The expected taxonomic range for this enzyme is: Bacteria, Archaea
Synonyms
d-xylonate dehydratase, xylonate dehydratase, ccxydht, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D-xylo-aldonate dehydratase
-
-
-
-
D-xylonate dehydratase
-
-
-
-
dehydratase, D-xylonate
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C-O bond cleavage by elimination of water
-
-
-
-
PATHWAY SOURCE
PATHWAYS
-
-, -, -, -, -
SYSTEMATIC NAME
IUBMB Comments
D-xylonate hydro-lyase (2-dehydro-3-deoxy-D-xylonate-forming)
-
CAS REGISTRY NUMBER
COMMENTARY hide
84788-77-2
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
D-xylonate
2-dehydro-3-deoxy-D-arabinonate + H2O
show the reaction diagram
-
-
-
?
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
D-xylonate
2-dehydro-3-deoxy-D-arabinonate + H2O
show the reaction diagram
-
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Mg2+
5 mM, required for activity, activates
Mn2+
5 mM, required for activity, activates
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2-mercaptoethanol
1 mM, 44% loss of activity
dithiothreitol
1 mM, 70% loss of activity
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
4.88
D-xylonate
pH 8.0, 30°C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.7 - 8.5
pH 6.7: about 65% of maximal activity, pH 8.5: about 65% of maximal activity
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
20 - 42
20°C: about 60% of maximal activity, 42°C: about 50% of maximal activity, activity is almost undetectable above 60x01C°
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
SwissProt
Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
70000
SDS-PAGE
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
70
the enzyme is denatured to precipitation above 70°C
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Jiang, Y.; Liu, W.; Cheng, T.; Cao, Y.; Zhang, R.; Xian, M.
Characterization of D-xylonate dehydratase YjhG from Escherichia coli
Bioengineered
6
227-232
2015
Escherichia coli (P39358), Escherichia coli, Escherichia coli K12 (P39358)
Manually annotated by BRENDA team