Enzymes responsible for metabolism of Nα-benzyloxycarbonyl-l-lysine in microorganisms
スポンサーリンク
概要
- 論文の詳細を見る
The present paper reviews the enzymes catalyzing conversion of Nα-benzyloxycarbonyl-l-lysine (Nα-Z-l-lysine) to Nα-benzyloxycarbonyl-l-aminoadipic acid (Nα-Z-l-AAA) in fungal and bacterial strains. Aspergillus niger AKU 3302 and Rhodococcus sp. AIU Z-35-1 converted Nα-Z-l-lysine to Nα-Z-l-AAA via Nα-benzyloxycarbonyl-l-aminoadipate-δ-semialdehyde (Nα-Z-l-AASA). However, different enzyme combinations were involved in the Nα-Z-l-lysine metabolism of both strains. A. niger strain converted Nα-Z-l-lysine to Nα-Z-l-AASA by amine oxidase, and the resulting Nα-Z-l-AASA was converted to Nα-Z-l-AAA by an aldehyde oxidase. In the Rhodococcus strain, conversion of Nα-Z-l-lysine to Nα-Z-l-AASA was catalyzed by l-specific amino acid oxidase. The resulting Nα-Z-l-AASA was converted to Nα-Z-l-AAA by an aldehyde dehydrogenase. The present paper also describes characteristics of new enzymes obtained from those strains.
論文 | ランダム
- Proline Effect on the Thermostability and Slow Unfolding of a Hyperthermophilic Protein
- 2P-078 大腸菌由来pitrilysinの安定性解析(蛋白質・物性(2),第46回日本生物物理学会年会)
- Structural Basis for the Decarboxylation of Orotidine 5'-Monophosphate (OMP) by Plasmodium Falciparum OMP Decarboxylase
- Protein Thermostabilization Requires a Fine-tuned Placement of Surface-charged Residues
- Application of Femtosecond Laser Ablation for Detaching Grown Protein Crystals from Glass Capillary Tube(METHODS)