NADP-specific glutamate dehydrogenase of Penicillium chrysogenum has a homohexamer structure.
The NADP-specific glutamate dehydrogenase of a high beta-lactam producing industrial strain of Penicillium chrysogenum was purified to homogeneity. The enzyme (M(r) = 339,000 +/- 34,000) was demonstrated to have a homohexamer quaternary structure with a subunit molecular mass of M(r) = 56,000 +/- 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.
Department of Microbiology and Biotechnology, Kossuth Lajos University, Debrecen, Hungary.
M S
MS
Bogáti
I
I
Pócsi
J
J
Maticsek
P
P
Boross
J
J
Tözsér
A
A
Szentirmai
D000595:Amino Acid Sequence; D018086:Glutamate Dehydrogenase (NADP+) / Q000737:chemistry*; D008969:Molecular Sequence Data; D008970:Molecular Weight; D010408:Penicillium chrysogenum / Q000201:enzymology*; D011487:Protein Conformation; D017421:Sequence Analysis; D017386:Sequence Homology, Amino Acid
D018086:Glutamate Dehydrogenase (NADP+)