The enzyme ADP-dependent short-chain-acyl-CoA hydrolase (EC 3.1.2.18)

catalyzes Catalysis () is the increase in rate of a chemical reaction due to an added substance known as a catalyst (). Catalysts are not consumed by the reaction and remain unchanged after it. If the reaction is rapid and the catalyst recycles quick ...

the reaction :acyl-CoA + H₂O

\rightleftharpoons

CoA + a carboxylate This enzyme belongs to the family of

hydrolase In biochemistry, hydrolases constitute a class of enzymes that commonly function as biochemical catalysts that use water to break a chemical bond: :\ce \quad \xrightarrowtext\quad \ce This typically results in dividing a larger molecule into s ...

s, specifically those acting on

thioester In organic chemistry, thioesters are organosulfur compounds with the molecular structure . They are analogous to carboxylate esters () with the sulfur in the thioester replacing oxygen in the carboxylate ester, as implied by the thio- prefix ...

bonds. The

systematic name A systematic name is a name given in a systematic way to one unique group, organism, object or chemical substance, out of a specific population or collection. Systematic names are usually part of a nomenclature. A semisystematic name or semitrivi ...

of this enzyme class is ADP-dependent-short-chain-acyl-CoA hydrolase. Other names in common use include short-chain acyl coenzyme A hydrolase, propionyl coenzyme A hydrolase, propionyl-CoA hydrolase, propionyl-CoA thioesterase, short-chain acyl-CoA hydrolase, and short-chain acyl-CoA thioesterase. It employs one cofactor, ADP. At least one compound,

NADH Nicotinamide adenine dinucleotide (NAD) is a coenzyme central to metabolism. Found in all living cells, NAD is called a dinucleotide because it consists of two nucleotides joined through their phosphate groups. One nucleotide contains an ade ...

is known to inhibit this enzyme.

References

* * EC 3.1.2 Enzymes of unknown structure {{3.1-enzyme-stub