MECHANISM AND STEREOCHEMISTRY OF ENZYMIC REACTIONS INVOLVED IN PORPHYRIN BIOSYNTHESIS
MECHANISM AND STEREOCHEMISTRY OF ENZYMIC REACTIONS INVOLVED IN PORPHYRIN BIOSYNTHESIS
复制标题
DOI:
10.1098/rstb.1976.0005
复制
发表时间:
1976-01-01
期刊:
影响因子:
--
通讯作者:
ZAMAN, Z
中科院分区:
文献类型:
--
作者:
AKHTAR, M;ABBOUD, MM;ZAMAN, Z
5-Aminolaevulinate synthetase catalyses the condensation of glycine and succinyl-CoA to give 5-aminolaevulinic acid. At least two broad pathways may be considered for the initial C—C bond forming step in the reaction. In pathway A the Schiff base of glycine and enzyme bound pyridoxal phosphate (a) undergoes decarboxylation to give the carbanion (b) which then condenses with succinyl-CoA with the retention of both the original C2 hydrogen atoms of glycine. In pathway B, loss of a C2 hydrogen atom gives another type of carbanion (c) that reacts with succinyl-CoA. Evidence has been presented to show that the initial C—C bond forming event occurs via pathway B which involves the removal of the proRhydrogen atom of glycine. Subsequent mechanistic and stereochemical events occurring at the carbon atom destined to become C5 of 5-aminolaevulinate have also been delineated.