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δ‐Aminolevulinic acid biosynthesis in Ustilago maydis
Author(s) -
Schneegurt Mark A.
Publication year - 2005
Publication title -
journal of basic microbiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.58
H-Index - 54
eISSN - 1521-4028
pISSN - 0233-111X
DOI - 10.1002/jobm.200410479
Subject(s) - ustilago , biochemistry , glycine , biosynthesis , enzyme , yeast , bacteria , chemistry , glutamate synthase , glutamate receptor , biology , glutamate dehydrogenase , amino acid , gene , genetics , receptor
A biosynthetic precursor of tetrapyrroles, δ‐aminolevulinic acid (ALA), can be formed via two pathways: enzymatic condensation of glycine and succinyl‐CoA by ALA synthase in animal mitochondria and some fungi, and the C 5 pathway converting glutamate to ALA in plants, algae, archaea, and most bacteria. The two pathways are distinguishable using specifically radiolabeled compounds. The C 1 of glutamate is lost during conversion to succinate in the TCA cycle, and the C 2 of glycine is lost during conversion to acetyl‐CoA on the way to glutamate. Desalted high‐speed supernatants of Ustilago maydis sporidia extracts were assayed using specifically radiolabeled substrates. A significant amount of radiolabel was incorporated into ALA from 2‐[ 14 C]glycine. No radiolabel was incorporated into ALA from 1‐[ 14 C]glutamate. These results indicate that the basidiomycete yeast, Ustilago maydis , has active ALA synthase. (© 2005 WILEY‐VCH Verlag GmbH & Co. KGaA, Weinheim)