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NADP‐specific glutamate dehydrogenase of Penicillium chrysogenum has a homohexamer structure
Author(s) -
Bogáti Magdolna Sz.,
Pócsi István,
Maticsek Judit,
Boross Péter,
Tózsér József,
Szentirmai Attila
Publication year - 1996
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.3620360512
Subject(s) - penicillium chrysogenum , glutamate dehydrogenase , enzyme , biochemistry , protein quaternary structure , biology , thermophile , dehydrogenase , strain (injury) , molecular mass , protein subunit , chemistry , stereochemistry , glutamate receptor , gene , receptor , anatomy
The NADP‐specific glutamate dehydrogenase of a high β‐lactam producing industrial strain of Penicillium chrysogenum was purified to homogeneity. The enzyme (M r = 339000 ± 34000) was demonstrated to have a homohexamer quaternary structure with a subunit molecular mass of M r = 56000 ± 2000. The N‐terminal sequence of the enzyme was also determined and was found to be highly homologous to other fungal NADP‐specific glutamate dehydrogenase sequences.