A divalent cation is essential for activity. Mn2+ (2--6 mM) is most effective.
The enzyme controls intracellular levels of P1,P5-bis(5'-adenosyl)pentaphosphate and P1,P6-bis(5'-adenosyl)hexaphosphate. Weak activity with P1,P4-bis(5'-adenosyl)tetraphosphate. Marked preference for adenine over guanine nucleotides.
A divalent cation is essential for activity. Mn2+ (2--6 mM) is most effective.
The enzyme controls intracellular levels of P1,P5-bis(5'-adenosyl)pentaphosphate and P1,P6-bis(5'-adenosyl)hexaphosphate. Weak activity with P1,P4-bis(5'-adenosyl)tetraphosphate. Marked preference for adenine over guanine nucleotides.
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
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
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
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
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
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
diadenosine tetraphosphate and diadenosine triphosphate, adenosine nucleotides, diphosphoinositol polyphosphate and phosphoribosyl pyrophosphate are not hydrolyzed
diadenosine tetraphosphate and diadenosine triphosphate, adenosine nucleotides, diphosphoinositol polyphosphate and phosphoribosyl pyrophosphate are not hydrolyzed
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
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
a divalent cation is essential for activity, with Mn2+ by far the most effective between 2 and 6 mM. Cu2+ supports less than 30% and Zn2+ and Co2+ each less than 3% of the maximum activity
a divalent cation is essential for activity, with Mn2+ by far the most effective between 2 and 6 mM. Cu2+ supports less than 30% and Zn2+ and Co2+ each less than 3% of the maximum activity
a divalent cation is essential for activity, with Mn2+ by far the most effective between 2 and 6 mM. Cu2+ supports less than 30% and Zn2+ and Co2+ each less than 3% of the maximum activity
a divalent cation is essential for activity, with Mn2+ by far the most effective between 2 and 6 mM. Cu2+ supports less than 30% and Zn2+ and Co2+ each less than 3% of the maximum activity
Bioinformatics Analysis Reveals an Association Between Cancer Cell Stemness, Gene Mutations, and the Immune Microenvironment in Stomach Adenocarcinoma.
no signal for hAps1 is detected in placenta, liver, skeletal muscle, kidney, spleen, colon or peripheral blood leukocytes. No activity in breast GI-101 cells, lung LX-1 cells, colon CX-1 cells, lung GI-117 cells, colon GI-112 cells and pancreas GI-103 cells
no signal for hAps1 is detected in placenta, liver, skeletal muscle, kidney, spleen, colon or peripheral blood leukocytes. No activity in breast GI-101 cells, lung LX-1 cells, colon CX-1 cells, lung GI-117 cells, colon GI-112 cells and pancreas GI-103 cells
no signal for hAps1 is detected in placenta, liver, skeletal muscle, kidney, spleen, colon or peripheral blood leukocytes. No activity in breast GI-101 cells, lung LX-1 cells, colon CX-1 cells, lung GI-117 cells, colon GI-112 cells and pancreas GI-103 cells
no signal for hAps2 is found in skeletal muscle, thymus, small intestine, colon or peripheral blood leukocytes. No activity in tumour cell lines from breast GI-101, lung LX-1, colon CX-1, lung GI-117, colon GI-112 and pancreas GI-103
no signal for hAps2 is found in skeletal muscle, thymus, small intestine, colon or peripheral blood leukocytes. No activity in tumour cell lines from breast GI-101, lung LX-1, colon CX-1, lung GI-117, colon GI-112 and pancreas GI-103
no signal for hAps2 is found in skeletal muscle, thymus, small intestine, colon or peripheral blood leukocytes. No activity in tumour cell lines from breast GI-101, lung LX-1, colon CX-1, lung GI-117, colon GI-112 and pancreas GI-103
the content of acid-soluble and acid-insoluble polyphosphates under DDP1 overexpression decreases by 9 and 28%, respectively. The average chain length of salt-soluble and alkali-soluble fractions does not change in the overexpressing strain, and that of acid-soluble polyphosphate increases under phosphate excess. At the initial stage of polyphosphate recovery after phosphorus starvation, the chain length of the acid-soluble fraction in transformed cells is lower compared to the recipient strain. In DDP1 deletion mutant, the level of inositol pyrophosphate is twice higher, while the level of polyphosphate is reduced. The overexpression of DDP1 probably leads to a decrease in the level of diphosphoinositol pentakisphosphate and bis(diphosphoinositol) tetrakisphosphate in the cell. These compounds seem to be involved in the regulation of polyphosphate synthesis and degradation
diphosphoinositol polyphosphate phosphohydrolase (DDP1, EC 3.6.1.52) is also a diadenosine hexaphosphate hydrolase (AMP-forming) (EC 3.6.1.60) and shows endopolyphosphatase (EC 3.6.1.10) activity. The relationship between inositol pyrophosphate and polyphosphate metabolisms seems to be complicated
yeast diphosphoinositol polyphosphate phosphohydrolase (DDP1) having endopolyphosphatase activity on inorganic polyphosphate metabolism in Saccharomyces cerevisiae. Complex nature of DDP1 involvement in the regulation of polyphosphate content and chain length in yeasts
overexpression of yeast diphosphoinositol polyphosphate phosphohydrolase (DDP1) in Saccharomyces cerevisiae leads to significantly increased compared to the parent strain. The content of acid-soluble and acid-insoluble polyphosphates under DDP1 overexpression decreases by 9 and 28%, respectively
overexpression of yeast diphosphoinositol polyphosphate phosphohydrolase (DDP1) in Saccharomyces cerevisiae leads to significantly increased compared to the parent strain. The content of acid-soluble and acid-insoluble polyphosphates under DDP1 overexpression decreases by 9 and 28%, respectively
gene DDP1, recombinant overexpression in Saccharomyces cerevisiae strain CRN. The initial strain CRN lacks the endopolyphosphatase PPN1, but has its own protein DDP1, which accounts for the low endopolyphosphatase activity in this strain. The recombinant DDP1 enzyme shows an endopolyphosphatase activity, the endopolyphosphatase activity of the transformant manifests itself both with long-chain polyP208 and with short-chain polyP15. Content of phosphate and polyphosphate in cells of CRN, overview
suppressing the expression of NUDT11, SLC22A3, and HNF1B influences cellular phenotypes associated with tumor-related properties in prostate cancer cells. 4 of the 12 known risk polymorphisms are strongly associated with transcripts NUDT11, MSMB, NCOA4, SLC22A3, and HNF1B in histologically normal tissue. Although associations are also observed in tumor tissue, they tend to be more attenuated
The diadenosine hexaphosphate hydrolases from Schizosaccharomyces pombe and Saccharomyces cerevisiae are homologues of the human diphosphoinositol polyphosphate phosphohydrolase. Overlapping substrate specificities in a MutT-type protein
Olejnik, K.; Murcha, M.W.; Whelan, J.; Kraszewska, E.
Cloning and characterization of AtNUDT13, a novel mitochondrial Arabidopsis thaliana Nudix hydrolase specific for long-chain diadenosine polyphosphates
The Saccharomyces cerevisiae YOR163w gene encodes a diadenosine 5', 5"'-P1,P6-hexaphosphate (Ap6A) hydrolase member of the MutT motif (Nudix hydrolase) family