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.

Delta-1-pyrroline-5-carboxylate synthase; Bifunctional enzyme that converts glutamate to glutamate 5- semialdehyde, an intermediate in the biosynthesis of proline, ornithine and arginine; In the C-terminal section; belongs to the gamma-glutamyl phosphate reductase family.

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.

Aminomethyltransferase, mitochondrial; The glycine cleavage system catalyzes the degradation of glycine; Belongs to the GcvT family.

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.

Argininosuccinate lyase; Belongs to the lyase 1 family. Argininosuccinate lyase subfamily.

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.

Glycine dehydrogenase (decarboxylating), mitochondrial; The glycine cleavage system catalyzes the degradation of glycine. The P protein (GLDC) binds the alpha-amino group of glycine through its pyridoxal phosphate cofactor; CO(2) is released and the remaining methylamine moiety is then transferred to the lipoamide cofactor of the H protein (GCSH) (By similarity). Belongs to the GcvP family.

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.

Glutaminase liver isoform, mitochondrial; Plays an important role in the regulation of glutamine catabolism. Promotes mitochondrial respiration and increases ATP generation in cells by catalyzing the synthesis of glutamate and alpha- ketoglutarate. Increases cellular anti-oxidant function via NADH and glutathione production. May play a role in preventing tumor proliferation.

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.

Histidine ammonia-lyase; Belongs to the PAL/histidase family.

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.

Homogentisate 1,2-dioxygenase.

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.

4-hydroxyphenylpyruvate dioxygenase; Key enzyme in the degradation of tyrosine; Belongs to the 4HPPD family.

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.

Kynurenine--oxoglutarate transaminase 3; Catalyzes the irreversible transamination of the L-tryptophan metabolite L-kynurenine to form kynurenic acid (KA). May catalyze the beta-elimination of S-conjugates and Se-conjugates of L- (seleno)cysteine, resulting in the cleavage of the C-S or C-Se bond (By similarity). Has transaminase activity towards L-kynurenine, tryptophan, phenylalanine, serine, cysteine, methionine, histidine, glutamine and asparagine with glyoxylate as an amino group acceptor (in vitro). Has lower activity with 2-oxoglutarate as amino group acceptor (in vitro).

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.

Kynureninase; Catalyzes the cleavage of L-kynurenine (L-Kyn) and L-3- hydroxykynurenine (L-3OHKyn) into anthranilic acid (AA) and 3- hydroxyanthranilic acid (3-OHAA), respectively. Has a preference for the L-3-hydroxy form. Also has cysteine-conjugate-beta-lyase activity.

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.

Methylmalonyl-CoA epimerase, mitochondrial; Belongs to the methylmalonyl-CoA epimerase family.

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.

Ornithine aminotransferase, mitochondrial.

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.

Phenylalanine-4-hydroxylase; Catalyzes the hydroxylation of L-phenylalanine to L-tyrosine. Belongs to the biopterin-dependent aromatic amino acid hydroxylase family.

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.

D-3-phosphoglycerate dehydrogenase; Catalyzes the reversible oxidation of 3-phospho-D-glycerate to 3-phosphonooxypyruvate, the first step of the phosphorylated L- serine biosynthesis pathway. Does not catalyze the reversible oxidation of 2-hydroxyglutarate to 2-oxoglutarate and the reversible oxidation of (S)-malate to oxaloacetate.

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.

Proline dehydrogenase 1, mitochondrial; Converts proline to delta-1-pyrroline-5-carboxylate.

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.

L-serine dehydratase/L-threonine deaminase; Belongs to the serine/threonine dehydratase family.

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.

Tyrosine aminotransferase; Transaminase involved in tyrosine breakdown. Converts tyrosine to p-hydroxyphenylpyruvate. Can catalyze the reverse reaction, using glutamic acid, with 2-oxoglutarate as cosubstrate (in vitro). Has much lower affinity and transaminase activity for phenylalanine. Belongs to the class-I pyridoxal-phosphate-dependent aminotransferase family.

Isobutyryl-CoA dehydrogenase, mitochondrial; Isobutyryl-CoA dehydrogenase which catalyzes one of the steps of the valine catabolic pathway. To a lesser extent, is also able to catalyze the oxidation of (2S)-2-methylbutanoyl-CoA.

Short/branched chain specific acyl-CoA dehydrogenase, mitochondrial; Has greatest activity toward short branched chain acyl-CoA derivative such as (s)-2-methylbutyryl-CoA, isobutyryl-CoA, and 2- methylhexanoyl-CoA as well as toward short straight chain acyl-CoAs such as butyryl-CoA and hexanoyl-CoA. Can use valproyl-CoA as substrate and may play a role in controlling the metabolic flux of valproic acid in the development of toxicity of this agent (By similarity).

Isobutyryl-CoA dehydrogenase, mitochondrial; Isobutyryl-CoA dehydrogenase which catalyzes one of the steps of the valine catabolic pathway. To a lesser extent, is also able to catalyze the oxidation of (2S)-2-methylbutanoyl-CoA.

Isovaleryl-CoA dehydrogenase, mitochondrial; Belongs to the acyl-CoA dehydrogenase family.

Isobutyryl-CoA dehydrogenase, mitochondrial; Isobutyryl-CoA dehydrogenase which catalyzes one of the steps of the valine catabolic pathway. To a lesser extent, is also able to catalyze the oxidation of (2S)-2-methylbutanoyl-CoA.

Propionyl-CoA carboxylase beta chain, mitochondrial; This is one of the 2 subunits of the biotin-dependent propionyl-CoA carboxylase (PCC), a mitochondrial enzyme involved in the catabolism of odd chain fatty acids, branched-chain amino acids isoleucine, threonine, methionine, and valine and other metabolites. Propionyl-CoA carboxylase catalyzes the carboxylation of propionyl- CoA/propanoyl-CoA to D-methylmalonyl-CoA/(S)-methylmalonyl-CoA (By similarity). Within the holoenzyme, the alpha subunit catalyzes the ATP-dependent carboxylation of the biotin carried by the biotin carboxyl carr [...]