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Information on EC 2.7.7.9 - UTP-glucose-1-phosphate uridylyltransferase and Organism(s) Danio rerio and UniProt Accession B8JMZ1

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Danio rerio
UNIPROT: B8JMZ1 not found.
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The taxonomic range for the selected organisms is: Danio rerio
The enzyme appears in selected viruses and cellular organisms
Synonyms
udp-glucose pyrophosphorylase, ugpase, udpg-pyrophosphorylase, udpgp, udp-glc pyrophosphorylase, udpglucose pyrophosphorylase, glucose-1-phosphate uridylyltransferase, udpg pyrophosphorylase, utp-glucose-1-phosphate uridylyltransferase, uridine diphosphoglucose pyrophosphorylase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
UDP-glucose pyrophosphorylase
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glucose 1-phosphate uridylyltransferase
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-
-
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glucose-1-phosphate uridylyltransferase
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-
-
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UDP glucose pyrophosphorylase
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-
-
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UDP-glucose pyrophosphorylase
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-
-
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UDPG phosphorylase
-
-
-
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UDPG pyrophosphorylase
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-
-
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UDPglucose pyrophosphorylase
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-
-
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uridine 5'-diphosphoglucose pyrophosphorylase
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-
-
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uridine diphosphate-D-glucose pyrophosphorylase
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-
-
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uridine diphosphoglucose pyrophosphorylase
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-
-
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uridine-diphosphate glucose pyrophosphorylase
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-
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uridylyltransferase, glucose 1-phosphate
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-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
nucleotidyl group transfer
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-
-
-
SYSTEMATIC NAME
IUBMB Comments
UTP:alpha-D-glucose-1-phosphate uridylyltransferase
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CAS REGISTRY NUMBER
COMMENTARY hide
9026-22-6
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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
UTP + alpha-D-glucose 1-phosphate
diphosphate + UDP-glucose
show the reaction diagram
-
-
-
r
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
UTP + alpha-D-glucose 1-phosphate
diphosphate + UDP-glucose
show the reaction diagram
-
-
-
r
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.183
alpha-D-glucose 1-phosphate
pH 7.5, 37°C, recombinant enzyme
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.5
assay at
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37
assay at
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
UniProt
Manually annotated by BRENDA team
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
B8JMZ1_DANRE
507
0
56878
TrEMBL
other Location (Reliability: 2)
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography and gel filtration
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression of His-tagged enzyme in Escherichia coli strain BL21(DE3)
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Yu, Q.; Zheng, X.
The crystal structure of human UDP-glucose pyrophosphorylase reveals a latch effect that influences enzymatic activity
Biochem. J.
442
283-291
2012
Drosophila melanogaster (A5XCL5), Danio rerio (B8JMZ1), Saccharomyces cerevisiae (C7GP37), Homo sapiens (Q16851), Homo sapiens, Caenorhabditis elegans (Q9XUS5)
Manually annotated by BRENDA team