A3626
Nα-Acetyl-L-ornithine
≥98% (TLC), suitable for ligand binding assays
Synonym(s):
N2-acetyl-L-lysine
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500 MG
$340.00
About This Item
Empirical Formula (Hill Notation):
C7H14N2O3
CAS Number:
Molecular Weight:
174.20
MDL number:
UNSPSC Code:
12352202
eCl@ss:
32160406
PubChem Substance ID:
NACRES:
NA.26
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Product Name
Nα-Acetyl-L-ornithine,
assay
≥98% (TLC)
Quality Level
form
powder
technique(s)
ligand binding assay: suitable
color
colorless to white
storage temp.
−20°C
SMILES string
CC(=O)N[C@@H](CCCN)C(O)=O
InChI
1S/C7H14N2O3/c1-5(10)9-6(7(11)12)3-2-4-8/h6H,2-4,8H2,1H3,(H,9,10)(H,11,12)/t6-/m0/s1
InChI key
JRLGPAXAGHMNOL-LURJTMIESA-N
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Biochem/physiol Actions
Nα-Acetyl-L-ornithine (AORN) is a substrate for the identification, differentiation and characterization of N(α)-acetyl-L-ornithine deacetylase(s) and of N-Acetyl-l-ornithine transcarbamylase(s) (AOTCase) found in plants, some eubacteria and some human pathogens.
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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Yongdong Li et al.
Biochemistry, 49(32), 6887-6895 (2010-08-11)
N-Acetyl-l-ornithine transcarbamylase (AOTCase), rather than ornithine transcarbamylase (OTCase), is the essential carbamylase enzyme in the arginine biosynthesis of several plant and human pathogens. The specificity of this unique enzyme provides a potential target for controlling the spread of these pathogens.
Dashuang Shi et al.
Proteins, 64(2), 532-542 (2006-06-03)
N-acetyl-L-ornithine transcarbamoylase (AOTCase) is a new member of the transcarbamoylase superfamily that is essential for arginine biosynthesis in several eubacteria. We report here crystal structures of the binary complexes of AOTCase with its substrates, carbamoyl phosphate (CP) or N-acetyl-L-ornithine (AORN)
Dashuang Shi et al.
The Journal of biological chemistry, 280(15), 14366-14369 (2005-02-26)
We have identified in Xanthomonas campestris a novel N-acetylornithine transcarbamylase that replaces ornithine transcarbamylase in the canonic arginine biosynthetic pathway of several Eubacteria. The crystal structures of the protein in the presence and absence of the reaction product, N-acetylcitrulline, were
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Biochimica et biophysica acta. Proteins and proteomics, 1869(2), 140561-140561 (2020-11-09)
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