| Literature DB >> 2543290 |
H J Op den Camp1, K D Liem, P Meesters, J M Hermans, C Van der Drift.
Abstract
Ammonia assimilation in Bacillus fastidiosus proceeds via the NADP-dependent glutamate dehydrogenase. The enzyme, purified to homogeneity, is composed of identical subunits with a molecular weight of about 48,000 dalton. Presumably the enzyme is a hexamer. The enzyme is specific for NADP(H). The pH optima for the amination and deamination reactions are 7.7 and 8.6, respectively. The temperature optimum is 60 degrees C. Furthermore, temperature stability and apparent Km values for substrates of both the amination and deamination reactions were determined. Several metabolites were tested for their effect on the enzyme activity. Only malate and fumarate showed some inhibitory effect.Entities:
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Year: 1989 PMID: 2543290 DOI: 10.1007/bf00398509
Source DB: PubMed Journal: Antonie Van Leeuwenhoek ISSN: 0003-6072 Impact factor: 2.271