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A1501

Sigma-Aldrich

N-Acetyl-D-methionin

~99%, suitable for ligand binding assays

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About This Item

Empirische Formel (Hill-System):
C7H13NO3S
CAS-Nummer:
1509-92-8
Molekulargewicht:
191.25
Beilstein:
1725553
EG-Nummer:
216-144-4
MDL-Nummer:
MFCD00069962
UNSPSC-Code:
12352209
eCl@ss:
32160406
PubChem Substanz-ID:
24890549
NACRES:
NA.26

product name

N-Acetyl-D-methionin, ~99%

Assay

~99%

Form

powder or crystals

Methode(n)

ligand binding assay: suitable

Farbe

white

mp (Schmelzpunkt)

102.3-103.6 °C

Lagertemp.

−20°C

SMILES String

CSCC[C@@H](NC(C)=O)C(O)=O

InChI

1S/C7H13NO3S/c1-5(9)8-6(7(10)11)3-4-12-2/h6H,3-4H2,1-2H3,(H,8,9)(H,10,11)/t6-/m1/s1

InChIKey

XUYPXLNMDZIRQH-ZCFIWIBFSA-N

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Anwendung

N-Acetyl-D-methionine may be used as a substrate to identify, differentiate and characterized N-acylamino acid racemase(s) and N-acyl-D-amino acid amidohydrolase(s).

Lagerklassenschlüssel

11 - Combustible Solids

WGK

WGK 3

Flammpunkt (°F)

Not applicable

Flammpunkt (°C)

Not applicable

Persönliche Schutzausrüstung

Eyeshields, Gloves, type N95 (US)

Analysenzertifikate (COA)

Suchen Sie nach Analysenzertifikate (COA), indem Sie die Lot-/Chargennummer des Produkts eingeben. Lot- und Chargennummern sind auf dem Produktetikett hinter den Wörtern ‘Lot’ oder ‘Batch’ (Lot oder Charge) zu finden.

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Wen-Ching Wang et al.
Journal of molecular biology, 342(1), 155-169 (2004-08-18)
N-acylamino acid racemase (NAAAR) catalyzes the racemization of N-acylamino acids and can be used in concert with an aminoacylase to produce enantiopure alpha-amino acids, a process that has potential industrial applications. Here we have cloned and characterized an NAAAR homologue
Pei-Hsun Lin et al.
European journal of biochemistry, 269(19), 4868-4878 (2002-10-02)
An N-acyl-d-amino acid amidohydrolase (N-D-AAase) was identified in cell extracts of a strain, Iso1, isolated from an environment containing N-acetyl-d-methionine. The bacterium was classified as Variovorax paradoxus by phylogenetic analysis. The gene was cloned and sequenced. The gene consisted of
S Pittelkow et al.
Protein expression and purification, 12(2), 269-276 (1998-03-31)
Aminoacylase I (EC 3.5.1.14) is one of the most abundant enzymes in the cortical region of mammalian kidney. Both the porcine and the human enzyme were overexpressed using baculovirus expression vector systems and purified by hydrophobic interaction chromatography and anion-exchange
T Odajima et al.
Cell biochemistry and function, 16(2), 139-147 (1998-06-24)
Urate oxidase from Candida utilis, an enzyme containing an essential thiol, was examined for its sensitivity to lactoperoxidase, an oxidant present in breast milk. Upon exposure to a system composed of lactoperoxidase, hydrogen peroxide and bromide at moderately alkaline pH
M J Wick et al.
Biochemical pharmacology, 37(7), 1225-1231 (1988-04-01)
Both N-hydroxy-2-acetamidofluorene (N-OH-AAF) and the heterocyclic analogue, 2-(N-hydroxyacetamido)carbazole (N-OH-AAC), were shown to be mechanism-based irreversible inhibitors (suicide inhibitors) of partially purified rat hepatic N-acetyltransferase (NAT) activity. Although N-OH-AAC exhibited an apparent first-order inactivation rate constant (ki) that was 7-fold lower
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