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5-Aminolevulinat sintaza

Izvor: Wikipedija
5-Aminolevulinat sintaza
5-Aminolevulinat sintaza dimer, Rhodobacter capsulatus
Identifikatori
EC broj 2.3.1.37
CAS broj 9037-14-3
IntEnz IntEnz view
BRENDA BRENDA entry
ExPASy NiceZyme view
KEGG KEGG entry
MetaCyc metabolic pathway
PRIAM profile
PDB RCSB PDB PDBe PDBj PDBsum

5-Aminolevulinat sintaza (EC 2.3.1.37, ALAS, ALA sintaza, alfa-aminolevulinsko kiselinska sintaza, delta-aminolevulinatna sintaza, delta-aminolevulinatna sintetaza, delta-aminolevulinsko kiselinska sintaza, delta-aminolevulinsko kiselinska sintetaza, delta-aminolevulinska sintetaza, 5-aminolevulinatna sintetaza, 5-aminolevulinsko kiselinska sintetaza, ALA sintetaza, aminolevulinatna sintaza, aminolevulinatna sintetaza, aminolevulinsko kiselinska sintaza, aminolevulinsko kiselinska sintetaza, aminolevulinska sintetaza) je enzim sa sistematskim imenom sukcinil-KoA:glicin C-sukciniltransferaza (dekarboksilacija).[1][2][3][4][5][6][7] Ovaj enzim katalizuje sledeću hemijsku reakciju

sukcinil-KoA + glicin 5-aminolevulinat + KoA + CO2

Ovaj enzim je piridoksal-fosfatni protein. Enzim u eritrocitima se genetički razlikuje od drugih tkiva.

Reference

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  1. Bishop, D.F., Henderson, A.S. and Astrin, K.H. (1990). „Human δ-aminolevulinate synthase - assignment of the housekeeping gene to 3p21 and the erythroid-specific gene to the X-chromosome”. Genomics 7: 207-214. PMID 2347585. 
  2. Kikuchi, G., Kumar, A., Talmage, P. and Shemin, D. (1958). „The enzymatic synthesis of δ-aminolevulinic acid”. J. Biol. Chem. 233: 1214-1219. PMID 13598764. 
  3. Ramaswamy, N.K. and Nair, P.M. (1973). „δ-Aminolevulinic acid synthetase from cold-stored potatoes”. Biochim. Biophys. Acta 293: 269-277. PMID 4685279. 
  4. Scholnick, P.L., Hammaker, L.E. and Marver, H.S. (1972). „Soluble δ-aminolevulinic acid synthetase of rat liver. I. Some properties of the partially purified enzyme”. J. Biol. Chem. 247: 4126-4131. PMID 4624703. 
  5. Scholnick, P.L., Hammaker, L.E. and Marver, H.S. (1972). „Soluble δ-aminolevulinic acid synthetase of rat liver. II. Studies related to the mechanism of enzyme action and hemin inhibition”. J. Biol. Chem. 247: 4132-4137. PMID 5035685. 
  6. Tait, G.H. (1973). „Aminolaevulinate synthetase of Micrococcus denitrificans. Purification and properties of the enzyme, and the effect of growth conditions on the enzyme activity in cells”. Biochem. J. 131: 389-403. PMID 4722442. 
  7. Warnick, G.R. and Burnham, B.F. (1971). „Regulation of porphyrin biosynthesis. Purification and characterization of δ-aminolevulinic acid synthase”. J. Biol. Chem. 246: 6880-6885. PMID 5315997. 

Literatura

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Spoljašnje veze

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