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Merck
CN

S7129

Sigma-Aldrich

O-Succinyl-L-homoserine

≥98.0% (TLC), suitable for ligand binding assays

Synonym(s):

L-Homoserine 4-(hydrogen butanedioate)

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About This Item

Empirical Formula (Hill Notation):
C8H13NO6
CAS Number:
1492-23-5
Molecular Weight:
219.19
MDL number:
MFCD00055782
UNSPSC Code:
12352209
PubChem Substance ID:
24899732
NACRES:
NA.26

Key Documents

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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

Related Categories

Storage Class Code

11 - Combustible Solids

WGK

WGK 3

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Personal Protective Equipment

dust mask type N95 (US), Eyeshields, Gloves

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Certificates of Analysis (COA)

Lot/Batch Number
0000203692
0000203693
0000162241
0000203692

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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
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
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
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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