aminolevulinate transaminase | |||||||||
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Identifiers | |||||||||
EC no. | 2.6.1.43 | ||||||||
CAS no. | 9012-46-8 | ||||||||
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 | ||||||||
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In enzymology, an aminolevulinate transaminase (EC 2.6.1.43) is an enzyme that catalyzes the chemical reaction
Thus, the two substrates of this enzyme are 5-aminolevulinate and pyruvate, whereas its two products are 4,5-dioxopentanoate and L-alanine.
This enzyme belongs to the family of transferases, specifically the transaminases, which transfer nitrogenous groups. The systematic name of this enzyme class is 5-aminolevulinate:pyruvate aminotransferase. Other names in common use include aminolevulinate aminotransferase, gamma,delta-dioxovalerate, aminotransferase, gamma,delta-dioxovaleric acid transaminase, 4,5-dioxovalerate aminotransferase, 4,5-dioxovaleric acid transaminase, 4,5-dioxovaleric transaminase, 5-aminolevulinic acid transaminase, alanine-gamma,delta-dioxovalerate aminotransferase, alanine-dioxovalerate aminotransferase, alanine:4,5-dioxovalerate aminotransferase, aminolevulinic acid transaminase, dioxovalerate transaminase, L-alanine-4,5-dioxovalerate aminotransferase, L-alanine:4,5-dioxovaleric acid transaminase, L-alanine:dioxovalerate transaminase, DOVA transaminase, and 4,5-dioxovaleric acid aminotransferase. This enzyme participates in porphyrin and chlorophyll metabolism. It employs one cofactor, pyridoxal phosphate.
Alanine transaminase (ALT) is a transaminase enzyme. It is also called alanine aminotransferase and was formerly called serum glutamate-pyruvate transaminase or serum glutamic-pyruvic transaminase (SGPT) and was first characterized in the mid-1950s by Arthur Karmen and colleagues. ALT is found in plasma and in various body tissues but is most common in the liver. It catalyzes the two parts of the alanine cycle. Serum ALT level, serum AST level, and their ratio are commonly measured clinically as biomarkers for liver health. The tests are part of blood panels.
Aminolevulinic acid synthase (ALA synthase, ALAS, or delta-aminolevulinic acid synthase) is an enzyme (EC 2.3.1.37) that catalyzes the synthesis of δ-aminolevulinic acid (ALA) the first common precursor in the biosynthesis of all tetrapyrroles such as hemes, cobalamins and chlorophylls. The reaction is as follows:
Transaminases or aminotransferases are enzymes that catalyze a transamination reaction between an amino acid and an α-keto acid. They are important in the synthesis of amino acids, which form proteins.
Porphobilinogen (PBG) is an organic compound that occurs in living organisms as an intermediate in the biosynthesis of porphyrins, which include critical substances like hemoglobin and chlorophyll.
Aminolevulinic acid dehydratase (porphobilinogen synthase, or ALA dehydratase, or aminolevulinate dehydratase) is an enzyme (EC 4.2.1.24) that in humans is encoded by the ALAD gene. Porphobilinogen synthase (or ALA dehydratase, or aminolevulinate dehydratase) synthesizes porphobilinogen through the asymmetric condensation of two molecules of aminolevulinic acid. All natural tetrapyrroles, including hemes, chlorophylls and vitamin B12, share porphobilinogen as a common precursor. Porphobilinogen synthase is the prototype morpheein.
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