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Cloning and sequencing of glutamate mutase component E from Clostridium tetanomorphum
Author(s) -
Brecht M.,
Kellermann J.,
Pluckthun A.
Publication year - 1993
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(93)80042-s
Subject(s) - biochemistry , protein subunit , mutase , homology (biology) , clostridium , nucleic acid sequence , amino acid , cloning (programming) , peptide sequence , biology , enzyme , chemistry , genetics , gene , bacteria , computer science , programming language
The nucleotide sequence of the large subunit E of glutamate mutase of Clostridium tetanomorphum was determined. The protein consists of 483 amino acids and is not made in a precursor form, thus excluding the possibility of subunit E being a pyruvoyl enzyme. It shows no homology to any other protein in the database, and while binding coenzyme B 2 , a conspicuous B 12 binding motif, shared amongst other proteins, is not detectable at the sequence level.