Article
Site-directed mutational analysis of the novel catalytic domains of alpha-aminoadipate reductase (Lys2p) from Candida albicans.
Molecular genetics and genomics : MGG - 1 May 2003
Guo S, Bhattacharjee J K
Abstract excerpt
The alpha-aminoadipate reductase, a novel enzyme in the alpha-aminoadipic acid pathway for the biosynthesis of lysine in fungi, catalyzes the conversion of alpha-aminoadipic acid to alpha-aminoadipic-delta-semialdehyde in the presence of ATP, NADPH and MgCl(2). This reaction requires two distinct gene products, Lys2p and Lys5p. In the presence of CoA, Lys5p posttranslationally activates Lys2p for the...
Topics
- Adenosine Triphosphate
- Aldehyde Oxidoreductases
- Amino Acid Sequence
- Candida albicans
- Catalytic Domain
- Escherichia coli
- Genotype
- L-Aminoadipate-Semialdehyde Dehydrogenase
- Lysine
- Models, Chemical
- Molecular Sequence Data
- Mutagenesis, Site-Directed
- NADP
- Plasmids
- Protein Structure, Tertiary
- Recombinant Proteins
- Sequence Homology, Amino Acid