A1501
N-Acetyl-D-methionine
~99%, suitable for ligand binding assays
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About This Item
Empirical Formula (Hill Notation):
C7H13NO3S
CAS Number:
Molecular Weight:
191.25
NACRES:
NA.26
PubChem Substance ID:
eCl@ss:
32160406
UNSPSC Code:
12352209
EC Number:
216-144-4
MDL number:
Beilstein/REAXYS Number:
1725553
Product Name
N-Acetyl-D-methionine, ~99%
InChI key
XUYPXLNMDZIRQH-ZCFIWIBFSA-N
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
SMILES string
CSCC[C@@H](NC(C)=O)C(O)=O
assay
~99%
form
powder or crystals
technique(s)
ligand binding assay: suitable
color
white
mp
102.3-103.6 °C
storage temp.
−20°C
Quality Level
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Application
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).
Storage Class
11 - Combustible Solids
wgk
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
Eyeshields, Gloves, type N95 (US)
Regulatory Information
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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
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
M Sugumaran et al.
Archives of insect biochemistry and physiology, 38(1), 44-52 (1998-05-20)
Incubation of catechol with mushroom tyrosinase in the presence of N-acetylmethionine resulted in the generation of an adduct. This product was identified to be N-acetylmethionyl catechol, on the basis of spectral characteristics and well-characterized chemical reaction of o-benzoquinone with N-acetylmethionine.
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
Kevin M Williams et al.
Journal of inorganic biochemistry, 99(11), 2119-2126 (2005-09-01)
The reaction of N-acetylmethionine (N-AcMet) with the complex [Pt(Et(2)en)(D(2)O)(2)](2+) (Et(2)en=N,N-diethylethylenediamine) was studied by NMR spectroscopy and molecular mechanics calculations. Complexes containing two methionine residues coordinated to the platinum atom were calculated to be relatively high in energy unless the bulk
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