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Information on EC 1.1.1.179 - D-xylose 1-dehydrogenase (NADP+, D-xylono-1,5-lactone-forming) and Organism(s) Haloarcula marismortui and UniProt Accession Q5UY95

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IUBMB Comments
The enzyme, characterized from pig arterial vessels and eye lens, also acts, more slowly, on L-arabinose and D-ribose. cf. EC 1.1.1.424, D-xylose 1-dehydrogenase (NADP+, D-xylono-1,4-lactone-forming).
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Haloarcula marismortui
UNIPROT: Q5UY95
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The taxonomic range for the selected organisms is: Haloarcula marismortui
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
nadp+-dependent d-xylose dehydrogenase, more
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
redox reaction
-
-
-
-
oxidation
-
-
-
-
reduction
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
D-xylose:NADP+ 1-oxidoreductase (D-xylono-1,5-lactone-forming)
The enzyme, characterized from pig arterial vessels and eye lens, also acts, more slowly, on L-arabinose and D-ribose. cf. EC 1.1.1.424, D-xylose 1-dehydrogenase (NADP+, D-xylono-1,4-lactone-forming).
CAS REGISTRY NUMBER
COMMENTARY hide
83534-37-6
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
D-glucose + NADP+
D-gluconolactone + NADPH + H+
show the reaction diagram
reaction is catalyzed with 70fold lower catalytic efficiency (kcat/KM) compared to activity with D-xylose + NADP*
-
-
?
D-ribose + NADP+
D-ribonolactone + NADPH + H+
show the reaction diagram
reaction is catalyzed with 1.8fold lower catalytic efficiency (kcat/KM) compared to activity with D-xylose + NADP*
-
-
?
D-xylose + NAD+
D-xylonolactone + NADH + H+
show the reaction diagram
Vmax/Km for NADP+ is 7fold higher than Vmax/KM for NAD+
-
-
?
D-xylose + NADP+
D-xylonolactone + NADPH + H+
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-xylose + NADP+
D-xylonolactone + NADPH + H+
show the reaction diagram
initial step in xylose degradation
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NAD+
Vmax/Km for NADP+ is 7fold higher than Vmax/KM for NAD+
NADP+
preferred electron acceptor. Vmax/Km for NADP+ is 7fold higher than Vmax/KM for NAD+
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
KCl
maximal activity at 1.5 M
MgCl2
maximal activity at 100 M
NaCl
maximal activity at 1.5 M
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
64
D-glucose
pH 8.3, 37°C
2.3
D-ribose
pH 8.3, 37°C
1.2
D-xylose
pH 8.3, 37°C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
273
D-glucose
pH 8.3, 37°C
360
D-ribose
pH 8.3, 37°C
356
D-xylose
pH 8.3, 37°C
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.043
D-glucose
pH 8.3, 37°C
1.57
D-ribose
pH 8.3, 37°C
2.97
D-xylose
pH 8.3, 37°C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7 - 9
more than 50% of maximal activity
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
25 - 50
activity increases exponentially with temperature between 25°C and 45°C. 50°C: optimum
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
175000
gel filtration
39900
4 * 39900, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homotetramer
4 * 39900, SDS-PAGE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
overexpression in Escherichia coli
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Johnsen, U.; Schonheit, P.
Novel xylose dehydrogenase in the halophilic archaeon Haloarcula marismortui
J. Bacteriol.
186
6198-6207
2004
Haloarcula marismortui (Q5UY95)
Manually annotated by BRENDA team