产品名称
O-琥珀酰-L-高丝氨酸,
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
assay
≥98.0% (TLC)
form
powder
technique(s)
ligand binding assay: suitable
color
white
storage temp.
−20°C
Quality Level
存储类别
11 - Combustible Solids
wgk
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
Eyeshields, Gloves, type N95 (US)
M Foglino et al.
Microbiology (Reading, England), 141 ( Pt 2), 431-439 (1995-02-01)
The relationship between genes and enzymes in the methionine biosynthetic pathway has been studied in Pseudomonas aeruginosa. The first step is catalysed by an O-succinylhomoserine synthase, the product of the metA gene mapped at 20 min on the chromosome. The
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
Susan M Aitken et al.
Archives of biochemistry and biophysics, 433(1), 166-175 (2004-12-08)
The ability of enzymes to catalyze specific reactions, while excluding others, is central to cellular metabolism. Control of reaction specificity is of particular importance for enzymes that employ catalytically versatile cofactors, of which pyridoxal 5'-phosphate is a prime example. Cystathionine
Susan M Aitken et al.
Biochemistry, 42(38), 11297-11306 (2003-09-25)
Cystathionine gamma-synthase (CGS) is a pyridoxal phosphate-dependent enzyme that catalyzes a gamma-replacement reaction, in which the succinyl group of an O-succinyl-L-homoserine (L-OSHS) is displaced by the thiol of L-cysteine to form L-cystathionine, in the first step of the bacterial transsulfuration
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)
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