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S7129

Sigma-Aldrich

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

Fórmula empírica (notación de Hill):
C8H13NO6
Número de CAS:
1492-23-5
Peso molecular:
219.19
MDL number:
MFCD00055782
UNSPSC Code:
12352209
PubChem Substance ID:
24899732
NACRES:
NA.26

product name

O-Succinyl-L-homoserine,

assay

≥98.0% (TLC)

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

Categorías relacionadas

Storage Class

11 - Combustible Solids

wgk_germany

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable

ppe

Eyeshields, Gloves, type N95 (US)

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P Vermeij et al.
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
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)
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
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
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
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