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Information on EC 3.6.1.21 - ADP-sugar diphosphatase
for references in articles please use BRENDA:EC3.6.1.21
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EC Tree 3 Hydrolases
3.6 Acting on acid anhydrides
3.6.1 In phosphorus-containing anhydrides
3.6.1.21 ADP-sugar diphosphatase
IUBMB Comments
Has a specificity that is distinct from that of UDP-sugar diphosphatase (EC 3.6.1.45).
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
- 3.6.1.21
- roundworm
- ascaris
- ascariasis
-
nudix
-
lung-stage
- glycogen
- adp-glucose
showSynonyms
asppase, adenosine diphosphate sugar pyrophosphatase, adp sugar pyrophosphatase, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
adenosine 5'-diphosphosugar pyrophosphatase
-
-
-
-
adenosine diphosphate-glucose pyrophosphatase
-
-
-
-
adenosine diphosphosugar pyrophosphatase
-
-
-
-
ADP-ribose pyrophosphatase
-
-
-
-
ADPsugar pyrophosphatase
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ADP-sugar + H2O = AMP + alpha-D-aldose 1-phosphate
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
phosphorous acid anhydride hydrolysis
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
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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
37289-32-0
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
ADP-alpha-D-glucose + H2O
AMP + alpha-D-glucose 1-phosphate
-
Substrates: -
Products: -
Products: -
?
ADP-mannose + H2O
AMP + alpha-D-mannose 1-phosphate
-
Substrates: -
Products: -
Products: -
?
ADP-ribose + H2O
AMP + alpha-D-ribose 1-phosphate
-
Substrates: -
Products: -
Products: -
?
GDP-Glc + H2O
GMP + Glc-1-phosphate
-
Substrates: very poor substrate
Products: -
Products: -
?
GDP-Man + H2O
GMP + Man-1-phosphate
-
Substrates: very poor substrate
Products: -
Products: -
?
ADP-glucose + H2O
AMP + alpha-D-glucose 1-phosphate
-
Substrates: -
Products: -
Products: -
?
ADP-glucose + H2O
AMP + alpha-D-glucose 1-phosphate
-
Substrates: -
Products: -
Products: -
?
ADP-sugar + H2O
AMP + sugar phosphate
-
Substrates: -
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme may play a pivotal role in controlling the gluconeogenic process and in interconnecting gluconeogenesis with other metabolic pathways
Products: -
Products: -
?
additional information
?
-
-
Substrates: no activity with UDPglucose, CDPglucose, GDPmannose, adenosine 5'-phosphosulfate, diphosphate, synthetic phosphodiester bonds containing compounds such as p-nitrophenylphosphate, sugar phosphates and nucleoside mono-, di- and triphosphates
Products: -
Products: -
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
additional information
?
-
-
Substrates: the enzyme may play a pivotal role in controlling the gluconeogenic process and in interconnecting gluconeogenesis with other metabolic pathways
Products: -
Products: -
?
ADP-sugar + H2O
AMP + sugar phosphate
-
Substrates: -
Products: -
Products: -
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mg2+
Mg2+
-
divalent cation required for full activity, Mg2+ at concentration of 0.4 mM most effective
Mg2+
-
divalent cation required for full activity, Mg2+ at concentration of 0.4 mM most effective
Mg2+
-
divalent cation required for full activity, Mg2+ at concentration of 0.4 mM most effective
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
intracellular inhibitor
-
can be destroyed by heating up to 58°C for a few min, inhibitor is resistant towards RNAse and DNAse and detectable at 280 nm
-
intracellular inhibitor
Salmonella weslaco
-
can be destroyed by heating up to 58°C for a few min, inhibitor is resistant towards RNAse and DNAse and detectable at 280 nm
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
D-glucose-1,6-bisphosphate
-
AspP activity is strongly enhanced by D-glucose-1,6-bisphosphate
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Ascariasis
Pyrophosphatase of the roundworm Ascaris suum plays an essential role in the worm's molting and development.
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
LITERATURE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7 - 8
7.8 - 8.4
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
58
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
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
brenda
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
partial
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Providenzia, R.; Bass, S.T.; Hansen, R.G.
A pyrophosphatase from mammalian tissues specific for derivatives of ADP
Biochim. Biophys. Acta
167
199-201
1968
Bos taurus, Oryctolagus cuniculus, Rattus norvegicus
brenda
Glaser, L.; Melo, A.; Paul, R.
Uridine diphosphate sugar hydrolase. Purification of enzyme and protein inhibitor
J. Biol. Chem.
242
1944-1954
1967
Escherichia coli, Salmonella enterica subsp. enterica serovar Typhimurium
brenda
Melo, A.; Glaser, L.
Nucleotide diphosphate hexose pyrophosphatases
Biochem. Biophys. Res. Commun.
22
524-531
1966
Escherichia coli, Salmonella weslaco
brenda
Moreno-Bruna, B.; Baroja-Fernandez, E.; Munoz, F.J.; Bastarrica-Berasategui, A.; Zandueta-Criado, A.; Rodriguez-Lopez, M.; Lasa, I.; Akazawa, T.; Pozueta-Romero, J.
Adenosine diphosphate sugar pyrophosphatase prevents glycogen biosynthesis in Escherichia coli
Proc. Natl. Acad. Sci. USA
98
8128-8132
2001
Escherichia coli
brenda
Moran-Zorzano, M.T.; Montero, M.; Munoz, F.J.; Alonso-Casajus, N.; Viale, A.M.; Eydallin, G.; Sesma, M.T.; Baroja-Fernandez, E.; Pozueta-Romero, J.
Cytoplasmic Escherichia coli ADP sugar pyrophosphatase binds to cell membranes in response to extracellular signals as the cell population density increases
FEMS Microbiol. Lett.
288
25-32
2008
Escherichia coli BL21(DE3)
brenda
EXTERNAL LINKS (specific for EC-Number 3.6.1.21)
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