Premium
5‐Aminolevulinic acid formation from glutamate via the C 5 pathway in Clostridium thermoaceticum
Author(s) -
Oh-hama T.,
Stolowich N.J.,
Scott A.I.
Publication year - 1988
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(88)80591-x
Subject(s) - chemistry , clostridium , glutamate receptor , biochemistry , stereochemistry , biology , bacteria , genetics , receptor
A cell‐free extract of the anaerobic eubacterium, Clostridium thermoaceticum , catalyses the synthesis of 5‐aminolevulinic acid (ALA) from glutamate via the C 5 pathway. The enzyme reaction resembles that of higher plants and algae in cofactor requirements and sensitivity to ribonuclease. From the phylogenetic distribution it is proposed that the C 5 pathway evolved earlier than the ALA synthase pathway.