English (United Kingdom)

https://curated-unify.zendy.io/wp-json/zendy-region/v1/featured_content/oa?rat=en

https://curated-unify.zendy.io/wp-json/zendy-region/v1/highlighted_journal/

Global: Zendy Plus annual

Presents the access of premium content as premium feature

Premium Content

Presents the keyphrase highlighting as premium feature

Keyphrase Highlighting

Presents the summarisation as premium feature

Summarisation

Insights

Presents the pdf analysis as premium feature

PDF Analysis

Presents the zaia usage as premium feature

ZAIA

Global: Zendy Tools annual

Global: Zendy Free Plan

Global: Zendy Tools monthly

Global: Zendy Plus monthly

NADP-glutamate dehydrogenase (EC 1.4.1.4:NADP-GDH) was purified to electrophoretic homogeneity from the multinuclear-unicellular green marine alga in Siphomales, Bryopsis maxima, and its properties were examined. M(r) of the undenatured enzyme was 280 kDa, and the enzyme is thought to be a hexamer of 46 kDa subunit protein. Optimum pHs for the reductive amination and oxidative deamination were 7.5 and 8.2-9.0 respectively. The enzyme displayed NADPH/NADH-specific activities with a ratio of 18:1. Apparent K(m) values for 2-oxoglutarate, ammonia, NADPH, glutamate and NADP+ were 3.0, 2.2, 0.03, 3.2 and 0.01 mM respectively. The enzymochemical characteristics of the GDH were studied and compared to those of other species. The B. maxima GDH was insensitive to 5 mM Ca(2+) and to 1 mM EDTA in contrast to higher plant NAD-GDHs. Chemical modifications with DTNB and pCMBS suggested that cysteine residues are essential for the enzymatic activity as in other species GDHs. The GDH was not affected by 1 mM purine nucleotides, suggesting that the enzyme is not allosteric, in contrast to animal NAD(P)-GDHs and fungal NAD-GDHs.

An NADP-Glutamate Dehydrogenase from the Green Alga Bryopsis maxima. Purification and Properties