504-91-6

Usage

Classification

Amino acid derivative

Potential applications

Treatment of metabolic disorders, precursor for synthesis of pharmaceutical compounds

Structure

Butanoic acid core with amino group at 2-position and aminoethoxy group at 4-position

InChI:InChI=1/C6H14N2O3/c7-2-4-11-3-1-5(8)6(9)10/h5H,1-4,7-8H2,(H,9,10)

Upstream product

• 220244-01-9 (2S,5R)-(-)-tert-butyl-6-amino-2-[(tert-butoxycarbonyl)amino]-5-hydroxyhexanoate 
• 321307-56-6 (R)-5-((S)-3-Amino-3-carboxy-propyl)-2,2-dimethyl-oxazolidine-3-carboxylic acid tert-butyl ester 
• 309928-96-9 (2S,5R)-6-azido-2-benzyloxycarbonylamino-5-hydroxyhexanoic acid 
• 56-87-1 L-lysine 
• 15366-19-5 methyl (S)-2-benzyloxycarbonylamino-6-diazo-5-oxohexanoate 
• 58456-27-2 (S)-3-(benzyloxycarbonyl)-4-(4-diazo-3-oxobutyl)-5-oxazolidinone 
• 309928-91-4 methyl (2S)-2-benzyloxycarbonylamino-6-bromo-5-oxohexanoate 
• 309928-94-7 (2S,5R)-5-azidomethyl-2-benzyloxycarbonylamino-δ-valerolactone 
• 309928-92-5 methyl (S)-6-azido-2-benzyloxycarbonylamino-5-oxohexanoate 
• 75466-93-2 DL-erythro-N²,N⁶-bis-benzyloxycarbonyl-5-hydroxy-lysine-lactone 
• 75466-93-2 DL-threo-N²,N⁶-bis-benzyloxycarbonyl-5-hydroxy-lysine-lactone 

Downstream Products

• 79432-14-7 (2S,5R)-2-amino-6-[(benzyloxycarbonyl)amino]-5-hydroxyhexanoic acid 
• 270089-67-3 (5R)-N^α-(fluoren-9-ylmethoxycarbonyl)-N^ε-benzyloxycarbonyl-5-O-(2,3,4,6-tetra-O-acetyl-β-D-galactopyranosyl)-5-hydroxy-L-lysine 
• 851857-30-2 (2S,5R)-2-Amino-6-benzyloxycarbonylamino-5-((2R,3R,4S,5S,6R)-3,4,5-triacetoxy-6-acetoxymethyl-tetrahydro-pyran-2-yloxy)-hexanoic acid 
• 107621-96-5 DL-threo-N²,N⁶-bis-(2,4-dinitro-phenyl)-5-hydroxy-lysine lactone 
• 95020-49-8 DL-threo-N²,N⁶-bis-(2,4-dinitro-phenyl)-5-hydroxy-lysine 
• 50439-45-7 (2S,5R)-5-hydroxy-2-piperidinecarboxylic acid 
• 63088-78-8 (2S,5R)-5-hydroxypiperidine-2-carboxylic acid 
• 2906-39-0 Δ¹-pyrroline-5-carboxylate 
• 334905-27-0 (3S,6S)-1-methyl-3-(tert-butyloxycarbonyl)aminohexahydro-6-(4-nitrophenylcarbonyl)oxy-2H-azepin-2-one 
• 334905-26-9 (3S,6S)-3-(tert-butyloxycarbonyl)aminohexahydro-6-(4-nitrophenylcarbonyl)oxy-2H-azepin-2-one 
• 104947-69-5 bengamide B 

Relevant academic research and scientific papers

Facile synthesis of 5-hydroxy-l-lysine from d-galactose as a chiral-precursor

A concise synthesis of (2S,5R) and (2S,5S)-5-hydroxy-lysine was achieved by utilizing d-galactose as a chiral-precursor with stereo retention. This synthetic strategy showcased the potential of utilizing carbohydrates as starting materials to prepare amino acids. Using the diazido intermediate, the derived β-d-galactopyranosyl and α-d-glucopyranosyl-(1→2)- β-d-galactosyl moieties were synthesized. This journal is the Partner Organisations 2014.

Biochemical characterisation and assessment of fibril-forming ability of collagens extracted from Bester sturgeon Huso huso × Acipenser ruthenus

Collagens purified from Bester sturgeon organs were characterised biochemically, and their fibril-forming abilities and fibril morphologies formed in vitro clarified. Yields of collagens were 2.1%, 11.9%, 0.4%, 18.1%, 0.4%, 0.8% and 0.03% (collagen dry weight/tissue wet weight) from scales, skin, muscle, swim bladder, digestive tract, notochord and snout cartilage, respectively. Using SDS-PAGE and amino acid composition analyses, collagens from scales, skin, muscle, the swim bladder and digestive tract were characterised as type I, and collagens from the notochord and snout cartilage as type II. Denaturation temperatures of the collagens, measured using circular dichroism, were 29.6, 26.8, 29.0, 32.9, 31.6 and 36.3 °C in scales, skin, muscle, swim bladder, digestive tract, and notochord, respectively. For fibril formation, swim bladder and skin collagen showed a more rapid rate of increase in turbidity, a shorter time to attain the maximum turbidity, and formed thicker fibrils compared with porcine tendon type I collagen.

The 2-Oxoglutarate-Dependent Oxygenase JMJD6 Catalyses Oxidation of Lysine Residues to give 5S-Hydroxylysine Residues

Amino acid analyses reveal that JMJD6-catalysed hydroxylation of RNA-splicing regulatory protein fragments occurs to give hydroxylysine products with 5S stereochemistry. This contrasts with collagen lysyl hydroxylases, which give 5R-hydroxylated products. The work suggests that more than one subfamily of lysyl hydroxylases has evolved and illustrates the importance of stereochemical assignments in proteomic analyses.

Synthesis of all four possible stereoisomers of 5-hydroxylysine

A simple protocol for the transformation of L- and D-glutamic acids into the enantiopure forms of all four isomers of 5-hydroxylysine is described. Copyright (C) 2000 Elsevier Science Ltd.

Stereoselective synthesis of (2R,5R)- and (2S,5R)-5-hydroxylysine

A stereoselective synthesis of (2S,5R)-5-hydroxylysine (1) and (2R,5R)-5-hydroxylysine (17), based on a concept involving Williams glycine template methodology and (R)-hydroxynitrile lyase for the introduction of chirality at the α-position and the side-chain, respectively, is described. This strategy offers an expeditious route towards orthogonally protected 5-hydroxylysines.

Collagen cross-links: Synthesis of pyridinoline, deoxypyridinoline and their analogues

An efficient chiral synthesis of (S,S)-(-)-3g, a key intermediate for the preparation of collagen cross-links pyridinoline (Pyd, 1) and deoxypyridinoline (Dpd, 2) was achieved from (4S)-5(tert-butoxy)-4-[(tert- butoxycarbonyl)amino]-5-oxopentanoic acid (21b). Quaternization of (S,S)-(- )-3g with iodide (2S, 5R)-(+)-4a followed by hydrolysiS provided a first chiral synthesis of natural (+)-Pyd (1). 1-(2S)-(+)-Pyd (1) was also synthesized from (S,S)-(-)-3g and iodide (2S, 5S)-(+)-4a. Similarly, quaternization of (S,S)-(-)-3g with iodide (2S)-(-)-4b, which was prepared from (2S)-(-)-6-amino-2[(tert-butoxycarbonyl)amino]hexanoic acid (31) in three steps, followed by hydrolysis afforded natural (+)-Dpd (2) in 5.3% overall yield. Also, the synthesis of racemic Dpd [(±)-2] and a variety of its analogues is presented.

3-Hydroxylysine, a potential marker for studying radical-induced protein oxidation

γ-Irradiation of several amino acids (Val, Leu, Ile, Lys, Pro, and Glu) in the presence of O2 generates hydroperoxides. We have previously isolated and characterized valine and leucine hydroperoxides, and hydroxides, and have detected these products in both isolated systems [e.g., bovine serum albumin (BSA) and human low-density lipoprotein (LDL)] and diseased human tissues (atherosclerotic plaques and lens cataractous proteins). This work was aimed at investigating oxidized lysine as a sensitive marker for protein oxidation, as such residues are present on protein surfaces, and are therefore likely to be particularly susceptible to oxidation by radicals in bulk solution. HO°attack on lysine in the presence of oxygen, followed by NaBH4 reduction, is shown to give rise to (2S)-3-hydroxylysine [(2S)-2,6-diamino-3- hydroxyhexanoic acid], (2S)-4-hydroxylysine [(2S)-2,6-diamino-4- hydroxyhexanoic acid], (2S,5R)5-hydroxylysine [(2S,5R)-2,6-diamino-5- hydroxyhexanoic acid], and (2S,5S)-5-hydroxylysine [(2S,5S)-2,6-diamino-5- hydroxyhexanoic acid]. 5-Hydroxylysines are natural products formed by lysyl oxidase and are therefore not good markers of radical-mediated oxidation. The other hydroxylysines are however useful markers, with HPLC analysis of 9- fluorenylmethyl chloroformate (FMOC) derivatives providing a sensitive and accurate method for quantitative measurement. Hydroxylysines have been detected in the hydrolysates of peptides (Gly-Lys-Gly and Lys-Val-Ile-Leu- Phe) and proteins (BSA and histone H1) exposed to HO°/O2, and subsequently treated with NaBH4. Quantification of the hydroxylysines yields, and comparison with hydroxyvalines and hydroxyleucines, supports the hypothesis that surface residues give higher yields of oxidized products than the hydrophobic leucines and valines, at least with globular proteins such as BSA. Hydroxylysines, and particularly 3-hydroxylysine, may therefore be sensitive and useful markers of radical-mediated protein oxidation in biological systems.