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추천 제품
제품명
O-Succinyl-L-homoserine,
분석
≥98.0% (TLC)
양식
powder
기술
ligand binding assay: suitable
색상
white
저장 온도
−20°C
SMILES string
N[C@@H](CCOC(=O)CCC(O)=O)C(O)=O
InChI
1S/C8H13NO6/c9-5(8(13)14)3-4-15-7(12)2-1-6(10)11/h5H,1-4,9H2,(H,10,11)(H,13,14)/t5-/m0/s1
InChI key
GNISQJGXJIDKDJ-YFKPBYRVSA-N
Storage Class Code
11 - Combustible Solids
WGK
WGK 3
Flash Point (°F)
Not applicable
Flash Point (°C)
Not applicable
개인 보호 장비
Eyeshields, Gloves, type N95 (US)
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시험 성적서(COA)
Lot/Batch Number
M Simon et al.
Journal of bacteriology, 153(1), 558-561 (1983-01-01)
Mutations were found which enable Escherichia coli K-12 to form homocysteine in the absence of cystathionase. The formation of homocysteine in the mutant strains required cystathionine gamma-synthetase, the metB gene product, but bypassed the normal intermediate cystathionine. It is concluded
Stefan Irmler et al.
Applied and environmental microbiology, 74(1), 99-106 (2007-11-13)
Volatile sulfur compounds are key flavor compounds in several cheese types. To better understand the metabolism of sulfur-containing amino acids, which certainly plays a key role in the release of volatile sulfur compounds, we searched the genome database of Lactobacillus
Yunhua Kong et al.
Journal of biochemistry, 143(1), 59-68 (2007-11-06)
Cystathionine gamma-synthase (CGS) catalyses the first step of the transsulfuration pathway that converts l-cysteine to l-homocysteine in bacteria, whereas this pathway is absent in human. In this report, we identified a new metB gene from Helicobacter pylori strain SS1, and
T Clausen et al.
The EMBO journal, 17(23), 6827-6838 (1998-12-08)
The transsulfuration enzyme cystathionine gamma-synthase (CGS) catalyses the pyridoxal 5'-phosphate (PLP)-dependent gamma-replacement of O-succinyl-L-homoserine and L-cysteine, yielding L-cystathionine. The crystal structure of the Escherichia coli enzyme has been solved by molecular replacement with the known structure of cystathionine beta-lyase (CBL)
Charles Ar Cotton et al.
eLife, 9 (2020-08-25)
The promiscuous activities of enzymes provide fertile ground for the evolution of new metabolic pathways. Here, we systematically explore the ability of E. coli to harness underground metabolism to compensate for the deletion of an essential biosynthetic pathway. By deleting
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