A3626
Nα-Acetyl-L-ornithine
≥98% (TLC), suitable for ligand binding assays
Synonym(s):
N2-acetyl-L-lysine
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About This Item
Empirical Formula (Hill Notation):
C7H14N2O3
CAS Number:
Molecular Weight:
174.20
UNSPSC Code:
12352202
eCl@ss:
32160406
PubChem Substance ID:
NACRES:
NA.26
MDL number:
Product Name
Nα-Acetyl-L-ornithine,
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
assay
≥98% (TLC)
form
powder
technique(s)
ligand binding assay: suitable
color
colorless to white
storage temp.
−20°C
Quality Level
Related Categories
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
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
Eyeshields, Gloves, type N95 (US)
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Daniel Charlier et al.
Amino acids, 51(8), 1103-1127 (2019-07-04)
Already very early, the study of microbial arginine biosynthesis and its regulation contributed significantly to the development of new ideas and concepts. Hence, the term "repression" was proposed by Vogel (The chemical basis of heredity, The John Hopkins Press, Baltimore
Séverine Lemarié et al.
Plant & cell physiology, 56(11), 2158-2168 (2015-09-13)
The role of salicylic acid (SA) and jasmonic acid (JA) signaling in resistance to root pathogens has been poorly documented. We assessed the contribution of SA and JA to basal and partial resistance of Arabidopsis to the biotrophic clubroot agent
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.
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
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)
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