S7129
O-Succinyl-L-homoserine
≥98.0% (TLC), suitable for ligand binding assays
Sinónimos:
L-Homoserine 4-(hydrogen butanedioate)
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About This Item
Productos recomendados
Nombre del producto
O-Succinyl-L-homoserine,
Ensayo
≥98.0% (TLC)
Nivel de calidad
Formulario
powder
técnicas
ligand binding assay: suitable
color
white
temp. de almacenamiento
−20°C
cadena SMILES
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
Clave InChI
GNISQJGXJIDKDJ-YFKPBYRVSA-N
Categorías relacionadas
Código de clase de almacenamiento
11 - Combustible Solids
Clase de riesgo para el agua (WGK)
WGK 3
Punto de inflamabilidad (°F)
Not applicable
Punto de inflamabilidad (°C)
Not applicable
Equipo de protección personal
Eyeshields, Gloves, type N95 (US)
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Journal of bacteriology, 181(18), 5833-5837 (1999-09-11)
Cysteine and methionine biosynthesis was studied in Pseudomonas putida S-313 and Pseudomonas aeruginosa PAO1. Both these organisms used direct sulfhydrylation of O-succinylhomoserine for the synthesis of methionine but also contained substantial levels of O-acetylserine sulfhydrylase (cysteine synthase) activity. The enzymes
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)
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
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
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
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