assay
≥98%
form
powder
color
white
storage temp.
−20°C
SMILES string
N[C@@H](CCCCN[C@@H](CCC(O)=O)C(O)=O)C(O)=O
InChI
1S/C11H20N2O6/c12-7(10(16)17)3-1-2-6-13-8(11(18)19)4-5-9(14)15/h7-8,13H,1-6,12H2,(H,14,15)(H,16,17)(H,18,19)/t7-,8-/m0/s1
InChI key
ZDGJAHTZVHVLOT-YUMQZZPRSA-N
Preparation Note
Prepared enzymatically
wgk
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
Eyeshields, Gloves, type N95 (US)
存储类别
11 - Combustible Solids
法规信息
新产品
此项目有
V V Rao et al.
Comparative biochemistry and physiology. B, Comparative biochemistry, 103(1), 221-224 (1992-09-01)
1. Developmental aspects of L-lysine-ketoglutarate reductase, the first enzyme in saccharopine pathway of L-lysine degradation in rat liver and brain tissues were studied. 2. Although the adult rat brain shows negligible activity, the enzyme activity was shown to be highly
Valeria Fochi et al.
The New phytologist, 213(1), 365-379 (2016-11-20)
Orchids are highly dependent on their mycorrhizal fungal partners for nutrient supply, especially during early developmental stages. In addition to organic carbon, nitrogen (N) is probably a major nutrient transferred to the plant because orchid tissues are highly N-enriched. We
A Stepansky et al.
Amino acids, 30(2), 121-125 (2006-03-10)
Lysine is a nutritionally important essential amino acid, whose synthesis in plants is strongly regulated by the rate of its synthesis. Yet, lysine level in plants is also finely controlled by a super-regulated catabolic pathway that catabolizes lysine into glutamate
Angie Sastoque et al.
Scientific reports, 10(1), 4860-4860 (2020-03-19)
The opportunistic pathogen Malassezia pachydermatis causes bloodstream infections in preterm infants or individuals with immunodeficiency disorders and has been associated with a broad spectrum of diseases in animals such as seborrheic dermatitis, external otitis and fungemia. The current approaches to
B Laber et al.
Analytical biochemistry, 181(2), 297-301 (1989-09-01)
A spectrophotometric assay for the activities of mesodiaminopimelate decarboxylase and L-alpha-amino-epsilon-caprolactam hydrolase is described. With the commercially available enzyme saccharopine dehydrogenase lysine formed either by decarboxylation of meso-diaminopimelate or by hydrolysis of L-alpha-amino-epsilon-caprolactam is converted to saccharopine with the concomitant
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