Information on EC 3.6.1.21 - ADP-sugar diphosphatase

for references in articles please use BRENDA:EC3.6.1.21
Word Map on EC 3.6.1.21
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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria

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EC NUMBER
COMMENTARY hide
3.6.1.21
-
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RECOMMENDED NAME
GeneOntology No.
ADP-sugar diphosphatase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
ADP-sugar + H2O = AMP + alpha-D-aldose 1-phosphate
show the reaction diagram
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-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
phosphorous acid anhydride hydrolysis
-
-
-
-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
d-mannose degradation
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-
Fructose and mannose metabolism
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-
Purine metabolism
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-
Starch and sucrose metabolism
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-
Metabolic pathways
-
-
Biosynthesis of secondary metabolites
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-
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SYSTEMATIC NAME
IUBMB Comments
ADP-sugar sugarphosphohydrolase
Has a specificity that is distinct from that of UDP-sugar diphosphatase (EC 3.6.1.45).
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CAS REGISTRY NUMBER
COMMENTARY hide
37289-32-0
-
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
-
-
Manually annotated by BRENDA team
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-
-
Manually annotated by BRENDA team
Salmonella weslaco
-
-
-
Manually annotated by BRENDA team
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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
ADP-alpha-D-glucose + H2O
AMP + alpha-D-glucose 1-phosphate
show the reaction diagram
-
-
-
-
?
ADP-Glc + H2O
AMP + Glc-1-phosphate
show the reaction diagram
ADP-glucose + H2O
AMP + alpha-D-glucose 1-phosphate
show the reaction diagram
-
-
-
-
?
ADP-Man + H2O
AMP + Man-1-phosphate
show the reaction diagram
ADP-mannose + H2O
AMP + alpha-D-mannose 1-phosphate
show the reaction diagram
-
-
-
-
?
ADP-Rib + H2O
AMP + Rib-5-phosphate
show the reaction diagram
ADP-ribose + H2O
AMP + alpha-D-ribose 1-phosphate
show the reaction diagram
-
-
-
-
?
ADP-sugar + H2O
AMP + sugar phosphate
show the reaction diagram
FAD + H2O
AMP + FMN
show the reaction diagram
GDP-Glc + H2O
GMP + Glc-1-phosphate
show the reaction diagram
-
very poor substrate
-
-
?
GDP-Man + H2O
GMP + Man-1-phosphate
show the reaction diagram
-
very poor substrate
-
-
?
NAD+ + H2O
AMP + NMN
show the reaction diagram
additional information
?
-
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
ADP-sugar + H2O
AMP + sugar phosphate
show the reaction diagram
additional information
?
-
-
the enzyme may play a pivotal role in controlling the gluconeogenic process and in interconnecting gluconeogenesis with other metabolic pathways
-
-
-
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
3-Phosphoglyceric acid
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-
diphosphate
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intracellular inhibitor
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additional information
-
no substantial inhibition by orthophosphate
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
D-glucose-1,6-bisphosphate
-
AspP activity is strongly enhanced by D-glucose-1,6-bisphosphate
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.29 - 1.9
ADP-Glc
0.167
ADP-glucose
-
pH 7.5
0.183
ADP-mannose
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pH 7.5
1.3
ADP-Rib
0.125
ADP-ribose
-
pH 7.5
40
GDP-Glc
-
same Km for GDP-Glc and GDP-Man
40
GDP-Man
-
same Km for GDP-Glc and GDP-Man
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.7
-
ADP-Glc with partially purified enzyme
6.6 - 7.2
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ADP-Glc as substrate
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.8 - 8.4
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5
-
no activity even in presence of Mg2+ or Co2+
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
-
AspP binds to cell membranes as the bacterial population density increases, 30% of the total enzyme remaining membrane associated as glycogen depletes during the stationary phase, binding of AspP to the cell membrane is not dependent on quorum-sensing autoinducer 2 or glucose availability
Manually annotated by BRENDA team
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
26000
-
2 * 26000, SDS-PAGE
40000 - 50000
-
gel filtration
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SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
-
2 * 26000, SDS-PAGE
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
partial
partial purification together with UDP-sugar pyrophosphatase
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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LINKS TO OTHER DATABASES (specific for EC-Number 3.6.1.21)
ExplorEnz
ExPASy
KEGG
MetaCyc
SABIO-RK
NCBI: PubMed, Protein, Nucleotide, Structure, Genome, OMIM
IUBMB Enzyme Nomenclature
PROSITE Database of protein families and domains
InterPro (database of protein families, domains and functional sites)