Pantothenate kinase 3; Plays a role in the physiological regulation of coenzyme A (CoA) levels; Belongs to the type II pantothenate kinase family.

Pantothenate kinase 2 (Hallervorden-Spatz syndrome).

4'-phosphopantetheine phosphatase; May play a role in the physiological regulation of coenzyme A (CoA) intracellular levels. The phosphatase activity shows preference for normal or oxidatively damaged intermediates of 4'- phosphopantetheine, which provides strong indirect evidence that the phosphatase activity pre-empts damage in the CoA pathway. Hydrolyzing excess 4'-phosphopantetheine could constitute a directed overflow mechanism to prevent its oxidation to the S-sulfonate, sulfonate, or other forms. Hydrolyzing 4'-phosphopantetheine sulfonate or S-sulfonate would forestall their co [...]

Vascular non-inflammatory molecule 3; Amidohydrolase that hydrolyzes specifically one of the carboamide linkages in D-pantetheine thus recycling pantothenic acid (vitamin B5) and releasing cysteamine; Belongs to the carbon-nitrogen hydrolase superfamily. BTD/VNN family.

Biotin--[propionyl-CoA-carboxylase [ATP-hydrolyzing]] ligase; Biotin--protein ligase catalyzing the biotinylation of the 4 biotin-dependent carboxylases acetyl-CoA-carboxylase, pyruvate carboxylase, propionyl-CoA carboxylase, and methylcrotonyl-CoA carboxylase.

Alpha-aminoadipic semialdehyde synthase, mitochondrial; Bifunctional enzyme that catalyzes the first two steps in lysine degradation. The N-terminal and the C-terminal contain lysine- oxoglutarate reductase and saccharopine dehydrogenase activity, respectively.

Glutamate dehydrogenase 1, mitochondrial; Mitochondrial glutamate dehydrogenase that converts L- glutamate into alpha-ketoglutarate. Plays a key role in glutamine anaplerosis by producing alpha-ketoglutarate, an important intermediate in the tricarboxylic acid cycle. May be involved in learning and memory reactions by increasing the turnover of the excitatory neurotransmitter glutamate; Belongs to the Glu/Leu/Phe/Val dehydrogenases family.

Cytochrome P450 4A14; A cytochrome P450 monooxygenase involved in the metabolism of fatty acids. Mechanistically, uses molecular oxygen inserting one oxygen atom into a substrate, and reducing the second into a water molecule, with two electrons provided by NADPH via cytochrome P450 reductase (CPR; NADPH-ferrihemoprotein reductase). Catalyzes the hydroxylation of saturated carbon hydrogen bonds of fatty acids. May act as a major omega- and ommega-1 hydroxylase for dodecanoic (lauric) acid in kidney. Catalyzes with low efficiency the epoxidation of 11,12-double bond of arachidonic acid.