serine-glyoxylate transaminase | |||||||||
---|---|---|---|---|---|---|---|---|---|
Identifiers | |||||||||
EC no. | 2.6.1.45 | ||||||||
CAS no. | 37259-57-7 | ||||||||
Databases | |||||||||
IntEnz | IntEnz view | ||||||||
BRENDA | BRENDA entry | ||||||||
ExPASy | NiceZyme view | ||||||||
KEGG | KEGG entry | ||||||||
MetaCyc | metabolic pathway | ||||||||
PRIAM | profile | ||||||||
PDB structures | RCSB PDB PDBe PDBsum | ||||||||
Gene Ontology | AmiGO / QuickGO | ||||||||
|
In enzymology, a serine-glyoxylate transaminase (EC 2.6.1.45) is an enzyme that catalyzes the chemical reaction
Thus, the two substrates of this enzyme are L-serine and glyoxylate, whereas its two products are 3-hydroxypyruvate and glycine.
This enzyme belongs to the family of transferases, specifically the transaminases, which transfer nitrogenous groups. The systematic name of this enzyme class is L-serine:glyoxylate aminotransferase. This enzyme participates in glycine, serine and threonine metabolism. It employs one cofactor, pyridoxal phosphate.
In enzymology, a glycerate dehydrogenase (EC 1.1.1.29) is an enzyme that catalyzes the chemical reaction
Glyoxylate reductase, first isolated from spinach leaves, is an enzyme that catalyzes the reduction of glyoxylate to glycolate, using the cofactor NADH or NADPH.
In enzymology, a hydroxypyruvate reductase (EC 1.1.1.81) is an enzyme that catalyzes the chemical reaction
The enzyme threonine aldolase is an enzyme that catalyzes the chemical reaction
In enzymology, a 2-aminoethylphosphonate—pyruvate transaminase is an enzyme that catalyzes the chemical reaction
In enzymology, 4-aminobutyrate transaminase, also called GABA transaminase or 4-aminobutyrate aminotransferase, or GABA-T, is an enzyme that catalyzes the chemical reaction:
In enzymology, an alanine-glyoxylate transaminase is an enzyme that catalyzes the chemical reaction
In enzymology, an alanine-oxo-acid transaminase is an enzyme that catalyzes the chemical reaction
In enzymology, an aromatic-amino-acid-glyoxylate transaminase is an enzyme that catalyzes the chemical reaction
In enzymology, an aspartate-prephenate aminotransferase is an enzyme that catalyzes the chemical reaction
In enzymology, a D-amino-acid transaminase is an enzyme that catalyzes the chemical reaction:
In enzymology, glutamate-prephenate aminotransferase is an enzyme that catalyzes the chemical reaction
In enzymology, a glycine-oxaloacetate transaminase is an enzyme that catalyzes the chemical reaction
In enzymology, a glycine transaminase is an enzyme that catalyzes the chemical reaction
In enzymology, a methionine-glyoxylate transaminase is an enzyme that catalyzes the chemical reaction
In enzymology, a serine-pyruvate transaminase is an enzyme that catalyzes the chemical reaction
In enzymology, a tryptophan transaminase is an enzyme that catalyzes the chemical reaction
Serine—pyruvate aminotransferase is an enzyme that in humans is encoded by the AGXT gene.
The glycine cleavage system (GCS) is also known as the glycine decarboxylase complex or GDC. The system is a series of enzymes that are triggered in response to high concentrations of the amino acid glycine. The same set of enzymes is sometimes referred to as glycine synthase when it runs in the reverse direction to form glycine. The glycine cleavage system is composed of four proteins: the T-protein, P-protein, L-protein, and H-protein. They do not form a stable complex, so it is more appropriate to call it a "system" instead of a "complex". The H-protein is responsible for interacting with the three other proteins and acts as a shuttle for some of the intermediate products in glycine decarboxylation. In both animals and plants, the glycine cleavage system is loosely attached to the inner membrane of the mitochondria. Mutations in this enzymatic system are linked with glycine encephalopathy.
4-aminobutyrate---pyruvate transaminase is an enzyme with systematic name 4-aminobutanoate:pyruvate aminotransferase. This enzyme is a type of GABA transaminase, which degrades the neurotransmitter GABA. The enzyme catalyses the following chemical reaction