What is ADP?

  • (noun): An ester of adenosine that is converted to ATP for energy storage.
    Synonyms: adenosine diphosphate
    See also — Additional definitions below

Some articles on adp:

ADP - Other
... Andorran peseta, a former currency of Andorra ADP, the IATA airport code for SLAF Anuradhapura, an airport in Sri Lanka Actual deferral percentage, a 401(k) test for highly ...
Starch Synthase
... synthase (EC 2.4.1.21) is an enzyme that catalyzes the chemical reaction ADP-glucose + (1,4-alpha-D-glucosyl)n ADP + (1,4-alpha-D-glucosyl)n+1 Thus, the two substrates of this enzyme are ADP ... The systematic name of this enzyme class is ADP-glucose1,4-alpha-D-glucan 4-alpha-D-glucosyltransferase ... Other names in common use include ADP-glucose-starch glucosyltransferase, adenosine diphosphate glucose-starch glucosyltransferase, adenosine diphosphoglucose-starc ...
ADP-specific Phosphofructokinase
... In enzymology, an ADP-specific phosphofructokinase (EC 2.7.1.146) is an enzyme that catalyzes the chemical reaction ADP + D-fructose 6-phosphate AMP + D-fructose 1,6-bisphosphate ... This enzyme is also called ADP-6-phosphofructokinase, ADP-dependent phosphofructokinase ...
Succinate-Co A Ligase (ADP-forming)
... In enzymology, a succinate-CoA ligase (ADP-forming) (EC 6.2.1.5) is an enzyme that catalyzes the chemical reaction ATP + succinate + CoA ADP + phosphate + succinyl-CoA ... name of this enzyme class is succinateCoA ligase (ADP-forming) ... Other names in common use include succinyl-CoA synthetase (ADP-forming), succinic thiokinase, succinate thiokinase, succinyl-CoA synthetase, succinyl coenzyme A synthetase (adenosine diphosphate-forming), succinyl ...
Sulfate Adenylyltransferase (ADP)
... In enzymology, a sulfate adenylyltransferase (ADP) (EC 2.7.7.5) is an enzyme that catalyzes the chemical reaction ADP + sulfate phosphate + adenylyl sulfate Thus, the two ... Other names in common use include ADP-sulfurylase, sulfate (adenosine diphosphate) adenylyltransferase, and adenosine diphosphate sulfurylase ...

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