S7129
O-Succinyl-L-homoserine
≥98.0% (TLC), suitable for ligand binding assays
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L-Homoserine 4-(hydrogen butanedioate)
C8H13NO6
Recommended Products
Assay
≥98.0% (TLC)
Quality Level
form
powder
technique(s)
ligand binding assay: suitable
color
white
storage temp.
−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
WGK
WGK 3
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
Personal Protective Equipment
dust mask type N95 (US), Eyeshields, Gloves
Certificates of Analysis (COA)
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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
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
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
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
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
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