Open AccessPurification and characterization of 5‐aminolevulinic acid dehydratase from Methanosarcina barken
Author(s) -
Bhosale Suresh,
Kshirsagar Deepa,
Pawar Prashant,
Yeole Tulsiram,
Ranade Dilip
Publication year - 1995
Publication title -
fems microbiology letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.899
H-Index - 151
eISSN - 1574-6968
pISSN - 0378-1097
DOI - 10.1111/j.1574-6968.1995.tb07465.x
Subject(s) - dehydratase , enzyme , biochemistry , cofactor , yeast , protein subunit , biology , methanosarcina , archaea , chemistry , gene
Abstract 5‐Aminolevulinic acid dehydratase from the archaebacterium Methanosarcina barken resembles the mammalian and yeast enzymes in its activation by Zn 2+ , whereas its activation by K + resembles the characteristic of bacterial enzymes. This enzyme is activated with Ni 2+ which is a component of F 430 , a cofactor present mainly in methanogens. The M r of 280000 for the native enzyme and 30 000 ± 2000 for the individual subunit suggest that the enzyme is composed of eight apparently indentical subunits similar to mammalian and yeast enzymes. The enzyme has two pH optima, at 8.5 and 9.4. Higher levels of 5‐aminolevulinic acid dehydratase in acetate‐grown cells suggest the possibility that regulation and control of this enzyme could be different on various growth substrates.