NADP-SPECIFIC GLUTAMATE-DEHYDROGENASE OF PENICILLIUM-CHRYSOGENUM HAS A HOMOHEXAMER STRUCTURE

Authors
BOGATI MS POCSI I MATICSEK J BOROSS P TOZSER J SZENTIRMAI A
Citation
Ms. Bogati et al., NADP-SPECIFIC GLUTAMATE-DEHYDROGENASE OF PENICILLIUM-CHRYSOGENUM HAS A HOMOHEXAMER STRUCTURE, Journal of basic microbiology, 36(5), 1996, pp. 371-375
Citations number
21
Categorie Soggetti
Microbiology
Journal title
Journal of basic microbiology → ACNP
ISSN journal
0233111X
Volume
36
Issue
5
Year of publication
1996
Pages
371 - 375
Database
ISI
SICI code
0233-111X(1996)36:5<371:NGOPHA>2.0.ZU;2-N
Abstract
The NADP-specific glutamate dehydrogenase of a high beta-lactam produc ing industrial strain of Penicillium chrysogenum was purified to homog eneity. 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 de termined and was found to be highly homologous to other fungal NADP-sp ecific glutamate dehydrogenase sequences.