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Archaebacterial malate dehydrogenase: The amino‐terminal sequence of the enzyme from Sulfolobus acidocaldarius is homologous to the eubacterial and eukaryotic malate dehydrogenases
Author(s) -
Görisch Helmut,
Jany Klaus-Dieter
Publication year - 1989
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(89)81348-1
Subject(s) - sulfolobus acidocaldarius , malate dehydrogenase , biochemistry , biology , sulfolobus , peptide sequence , enzyme , amino acid , dehydrogenase , archaea , gene
42 residues of the N‐terminal amino acid sequence of malate dehydrogenase from the thermoacidophilic archaebacterium Sulfolobus acidocaldarius have been determined as VKVAFIGVGRGVGQTIAYNTIVNGYADEVMLYDVVPELPTKK. In eubacterial and eukaryotic enzymes this region is known to encompass residues involved in pyridine nucleotide binding. In the archaebacterial enzyme the residues Gly‐7, Gly‐ 11 and Asp‐33 are also present. The data suggest that in the enzyme from S. acidocaldarius like in the other malate dehydrogenases the binding domain for NAD(H) is localized at the N‐terminal part of the polypeptide chain. The archaebacterial enzyme is homologous to the other malate dehydrogenases, of which the amino acid sequences are known, however, it is only distantly related to the mitochondrial/ E. coli group and the cytosolic/ Thermus flavus group.