3.6.1.60: diadenosine hexaphosphate hydrolase (AMP-forming)
This is an abbreviated version!
For detailed information about diadenosine hexaphosphate hydrolase (AMP-forming), go to the full flat file.
Word Map on EC 3.6.1.60
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3.6.1.60
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polyphosphates
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diphosphoinositol
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prostate
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autoantibody
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nudix
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serous
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nappa
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tumor-associated
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dipps
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phosphohydrolases
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trim39
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medicine
- 3.6.1.60
- polyphosphates
-
diphosphoinositol
- prostate
- autoantibody
-
nudix
-
serous
-
nappa
-
tumor-associated
- dipps
-
phosphohydrolases
- trim39
- medicine
Reaction
Synonyms
At3g26690, AtNUDT13, DDP1, diphosphoinositol polyphosphate phosphohydrolase, DIPP, hAps1, hAps2, More, NUDT10, NUDT11
ECTree
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Substrates Products
Substrates Products on EC 3.6.1.60 - diadenosine hexaphosphate hydrolase (AMP-forming)
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REACTION DIAGRAM
P1,P4-bis(5'-adenosyl)tetraphosphate + H2O
ATP + AMP
weak activity
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adenosine 5'-tetraphosphate + AMP
P1,P5-bis(5'-adenosyl)pentaphosphate is hydrolyzed at 40% of the activity compared to P1,P6-bis(5'-adenosyl)hexaphosphate
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P1,P5-bis(5'-adenosyl)pentaphosphate + H2O
adenosine 5'-tetraphosphate + AMP
marked preference for adenine over guanine nucleotides. The enzyme controls intracellular P1,P5-bis(5'-adenosyl)pentaphosphate and P1,P6-bis(5'-adenosyl)hexaphosphate levels
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P1,P5-bis(5'-adenosyl)pentaphosphate + H2O
adenosine 5'-tetraphosphate + AMP
marked preference for adenine over guanine nucleotides. The most rapidly metabolised substrate appears to be P1,P5-bis(5'-adenosyl)pentaphosphate, although P1,P6-bis(5'-adenosyl)hexaphosphate is bound with higher affinity
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P1,P5-bis(5'-adenosyl)pentaphosphate + H2O
adenosine 5'-tetraphosphate + AMP
the enzyme degrades P1,P6-bis(5'-adenosyl)hexaphosphate and P1,P5-bis(5'-adenosyl)pentaphosphate, in preference to other diadenosine polyphosphates
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P1,P5-bis(5'-adenosyl)pentaphosphate + H2O
adenosine 5'-tetraphosphate + AMP
the function of the enzyme may be to eliminate potentially toxic dinucleoside polyphosphates during sporulation
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P1,P5-bis(5'-adenosyl)pentaphosphate + H2O
adenosine 5'-tetraphosphate + AMP
hydrolysis of P1,P5-bis(5'-adenosyl)pentaphosphate yields predominantly AMP and adenosine tetraphosphate (96%)
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adenosine 5'-pentaphosphate + AMP
marked preference for adenine over guanine nucleotides. The enzyme controls intracellular P1,P5-bis(5'-adenosyl)pentaphosphate and P1,P6-bis(5'-adenosyl)hexaphosphate levels
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?
P1,P6-bis(5'-adenosyl)hexaphosphate + H2O
adenosine 5'-pentaphosphate + AMP
marked preference for adenine over guanine nucleotides. The most rapidly metabolised substrate appears to be P1,P5-bis(5'-adenosyl)pentaphosphate, although P1,P6-bis(5'-adenosyl)hexaphosphate is bound with higher affinity
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P1,P6-bis(5'-adenosyl)hexaphosphate + H2O
adenosine 5'-pentaphosphate + AMP
the predominant route of P1,P6-bis(5'-adenosyl)hexaphosphate hydrolysis is to AMP plus P1,P5-bis(5'-adenosyl)pentaphosphate, with the formation of ADP plus p4A being a more minor reaction. The enzyme degrades P1,P6-bis(5'-adenosyl)hexaphosphate and P1,P5-bis(5'-adenosyl)pentaphosphate, in preference to other diadenosine polyphosphates
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adenosine 5'-tetraphosphate + ADP
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P1,P6-bis(5'-adenosyl)hexaphosphate + H2O
adenosine 5'-tetraphosphate + ADP
preferred substrate. Hydrolysis of P1,P6-bis(5'-adenosyl)hexaphosphate with the formation of ADP or AMP
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P1,P6-bis(5'-adenosyl)hexaphosphate + H2O
adenosine 5'-tetraphosphate + ADP
the function of the enzyme may be to eliminate potentially toxic dinucleoside polyphosphates during sporulation
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?
P1,P6-bis(5'-adenosyl)hexaphosphate + H2O
adenosine 5'-tetraphosphate + ADP
hydrolysis in H218O shows that ADP and adenosine 5*-tetraphosphate are produced by attack at Pbeta and AMP and adenosine 5'-pentaphosphate are produced by attack at Palpha (76%) and AMP and adenosine 5'-pentaphosphate are produced by attack at Palpha (24%). P1,P6-bis(5'-adenosyl)hexaphosphate is a 8fold better substrate than P1,P5-bis(5'-adenosyl)pentaphosphate
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diadenosine tetraphosphate and diadenosine triphosphate, adenosine nucleotides, diphosphoinositol polyphosphate and phosphoribosyl pyrophosphate are not hydrolyzed
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additional information
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diadenosine tetraphosphate and diadenosine triphosphate, adenosine nucleotides, diphosphoinositol polyphosphate and phosphoribosyl pyrophosphate are not hydrolyzed
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additional information
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the enzyme also catalyses the hydrolysis of diphosphoinositol pentakisphosphate
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additional information
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no activity with P1,P4-bis(5'-adenosyl)tetraphosphate or other dinucleotides, mononucleotides, nucleotide sugars, or nucleotide alcohols
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additional information
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endopolyphosphatase activity is analyzed by the decrease in polyphosphate chain length (polyphosphate208 and polyphosphate15)
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