In biochemistry, a kinase is an enzyme that catalyzes the transfer of phosphate groups from high-energy, phosphate-donating molecules to specific substrates. This process is known as phosphorylation, where the high-energy ATP molecule donates a phosphate group to the substrate molecule. This transesterification produces a phosphorylated substrate and ADP. Conversely, it is referred to as dephosphorylation when the phosphorylated substrate donates a phosphate group and ADP gains a phosphate group. These two processes, phosphorylation and dephosphorylation, occur four times during glycolysis.
In cell biology, protein kinase A (PKA) is a family of serine-threonine kinase whose activity is dependent on cellular levels of cyclic AMP (cAMP). PKA is also known as cAMP-dependent protein kinase. PKA has several functions in the cell, including regulation of glycogen, sugar, and lipid metabolism. It should not be confused with 5'-AMP-activated protein kinase.
Acetyl-CoA carboxylase (ACC) is a biotin-dependent enzyme that catalyzes the irreversible carboxylation of acetyl-CoA to produce malonyl-CoA through its two catalytic activities, biotin carboxylase (BC) and carboxyltransferase (CT). ACC is a multi-subunit enzyme in most prokaryotes and in the chloroplasts of most plants and algae, whereas it is a large, multi-domain enzyme in the cytoplasm of most eukaryotes. The most important function of ACC is to provide the malonyl-CoA substrate for the biosynthesis of fatty acids. The activity of ACC can be controlled at the transcriptional level as well as by small molecule modulators and covalent modification. The human genome contains the genes for two different ACCs—ACACA and ACACB.
A serine/threonine protein kinase is a kinase enzyme, in particular a protein kinase, that phosphorylates the OH group of the amino-acid residues serine or threonine, which have similar side chains. At least 350 of the 500+ human protein kinases are serine/threonine kinases (STK).
The long chain fatty acyl-CoA ligase is an enzyme of the ligase family that activates the oxidation of complex fatty acids. Long chain fatty acyl-CoA synthetase catalyzes the formation of fatty acyl-CoA by a two-step process proceeding through an adenylated intermediate. The enzyme catalyzes the following reaction,
In enzymology, a [3-methyl-2-oxobutanoate dehydrogenase (acetyl-transferring)] is an enzyme that catalyzes the chemical reaction
In enzymology, a beta-adrenergic-receptor kinase is an enzyme that catalyzes the chemical reaction:
In enzymology, a dephospho-[reductase kinase] kinase is an enzyme that catalyzes the chemical reaction
In enzymology, an elongation factor 2 kinase is an enzyme that catalyzes the chemical reaction:
In enzymology, a glycerate kinase is an enzyme that catalyzes the chemical reaction
In enzymology, a Goodpasture-antigen-binding protein kinase is an enzyme that catalyzes the chemical reaction
In enzymology, a homoserine kinase is an enzyme that catalyzes the chemical reaction
In enzymology, a [isocitrate dehydrogenase (NADP+)] kinase (EC 2.7.11.5) is an enzyme that catalyzes the chemical reaction:
In enzymology, a low-density-lipoprotein receptor kinase is an enzyme that catalyzes the chemical reaction
In enzymology, a myosin-heavy-chain kinase is an enzyme that catalyzes the chemical reaction
In enzymology, a polo kinase is a kinase enzyme i.e. one that catalyzes the chemical reaction
In enzymology, a tau-protein kinase is an enzyme that catalyzes the chemical reaction
In enzymology, a tropomyosin kinase is an enzyme that catalyzes the chemical reaction
In enzymology, a [tyrosine 3-monooxygenase] kinase is an enzyme that catalyzes the chemical reaction
5'-AMP-activated protein kinase catalytic subunit alpha-1 is an enzyme that in humans is encoded by the PRKAA1 gene.
