504-21-2

Usage

Uses

Used in Pharmaceutical Industry:
(3S)-3,6-Diaminohexanoic acid is used as a therapeutic agent for the treatment of herpes simplex virus infections. It has been studied for its potential to inhibit viral replication and reduce the severity of symptoms.
Used in Nutraceutical Industry:
(3S)-3,6-Diaminohexanoic acid is used as a dietary supplement to support overall health and well-being. It contributes to the maintenance of healthy skin, bones, and the synthesis of carnitine, which helps in turning fat into energy.
Used in Cosmetic Industry:
(3S)-3,6-Diaminohexanoic acid is used as an ingredient in skincare products for its role in collagen formation and maintaining healthy skin. It helps improve skin elasticity and reduce the appearance of wrinkles and fine lines.
Used in Food and Beverage Industry:
(3S)-3,6-Diaminohexanoic acid is used as a nutritional additive in various food and beverage products to enhance their protein content and support overall health. It can be found in protein supplements, meal replacement shakes, and fortified foods.

InChI:InChI=1/C6H14N2O2/c7-3-1-2-5(8)4-6(9)10/h5H,1-4,7-8H2,(H,9,10)

Upstream product

• 86088-69-9 β-lysine di-N-phthaloyl methyl ester 
• 56-87-1 L-lysine 
• 70548-25-3 di-N-phthalimide l-ornithine 
• 118743-83-2 5-Acetoxy-3(S)-(4-benzyloxycarbonylaminobutyl)-N-<(R)-(-)-α-methylbenzyl>isoxazolidine 
• 118743-76-3 3(S)-(4-Benzyloxycarbonylaminobutyl)-N-<(R)-(-)-α-methylbenzyl>isoxazolidin-5-ol 
• 186581-53-3 diazomethane 
• 118743-79-6 (3S)-(4-Benzyloxycarbonylaminobutyl)-N-<(R)-(-)-α-methylbenzyl>isoxazolidin-5-one 
• 35107-12-1 (S)-N,N'-Dibenzyloxycarbonyl-β-lysine 
• 58773-34-5 5-deoxy-3-epi-negamycine 

Downstream Products

• 35761-12-7 (S)-3,6-bis-benzoylamino-hexanoic acid 
• 37682-58-9 (S)-6-Benzyloxycarbonylamino-3-((S)-3,6-bis-benzyloxycarbonylamino-hexanoylamino)-hexanoic acid methyl ester 
• 35107-12-1 (S)-N,N'-Dibenzyloxycarbonyl-β-lysine 
• 37682-54-5 (S)-3,6-Bis-benzyloxycarbonylamino-hexanoic acid benzyl ester 

Relevant academic research and scientific papers

Biochemical Characterization of an Arginine 2,3-Aminomutase with Dual Substrate Specificity

The radical S-adenosylmethionine (SAM) aminomutases represent an important pathway for the biosynthesis of β-amino acids. In this study, we report biochemical characterization of BlsG involved in blasticidin S biosynthesis as a radical SAM arginine 2,3-aminomutase. We showed that BlsG acts on both L-arginine and L-lysine with comparable catalytic efficiencies. Similar dual substrate specificity was also observed for the lysine 2,3-aminomutase from Escherichia coli (LAMEC). The catalytic efficiency of LAMEC is similar to that of BlsG, but is significantly lower than that of the enzyme from Clostridium subterminale (LAMCS), which acts only on L-lysine rather than on L-arginine. Moreover, we showed that enzymes can be grouped into two major phylogenetic clades, each corresponding to a certain C3 stereochemistry of the β-amino acid product. Our study expands the radical SAM aminomutase members and provides insights into enzyme evolution, supporting a trade-off between substrate promiscuity and catalytic efficiency.

How an enzyme tames reactive intermediates: Positioning of the active-site components of lysine 2,3-aminomutase during enzymatic turnover as determined by ENDOR spectroscopy

Lysine 2,3-aminomutase (LAM) utilizes a [4Fe-4S] cluster, S-adenosyl-L-methionine (SAM), and pyridoxal 5′-phosphate (PLP) to isomerize L-α-lysine to L-β-lysine. LAM is a member of the radical-SAM enzyme superfamily in which a [4Fe-4S]+ cluster reductively cleaves SAM to produce the 5′-deoxyadenosyl radical, which abstracts an H-atom from substrate to form 5′-deoxyadenosine (5′-Ado) and the α-Lys. radical (state 3 (Lys .)). This radical isomerizes to the β-Lys. radical (state 4(Lys.)), which then abstracts an H-atom from 5′-Ado to form β-lysine and the 5′-deoxyadenosyl radical; the latter then regenerates SAM. We use 13C, 1,2H, 31P, and 14N ENDOR to characterize the active site of LAM in intermediate states that contain the isomeric substrate radicals or analogues. With L-α-lysine as substrate, we monitor the state with β-Lys.. In parallel, we use two substrate analogues that generate stable analogues of the α-Lys. radical: trans-4,5-dehydro-L-lysine (DHLys) and 4-thia-L-lysine (SLys). This first glimpse of the motions of active-site components during catalytic turnover suggests a possible major movement of PLP during catalysis. However, the principal focus of this work is on the relative positions of the carbons involved in H-atom transfer. We conclude that the active site facilitates hydrogen atom transfer by enforcing van der Waals contact between radicals and their reacting partners. This constraint enables the enzyme to minimize and even eliminate side reactions of highly reactive species such as the 5′-deoxyadensosyl radical.

Asymmetric Syntheses of the Naturally Ocurring β-Amino Acids, β-Lysine, β-Leucine and β-Phenyl-β-alanine via Nitrone Cycloaddition

A general asymmetric synthesis of β-amino acids is based on the dipolar cycloaddition of nitrones 7 (R* chiral) with vinyl acetate 8a, ketene acetals 8b or α-chloroacrylonitrile 8c.The cycloadducts 9 are converted either directly (9b) or via the isoxazolidones 10 (9a, 9c) into the free β-amino acids 11.Diastereoselectivity at C-3 in the adducts 9 ranges between 2:1 and 11:1.The natural β-amino acids, β-lysine, β-leucine and β-phenyl-β-alanine, have been prepared in this way.

Enantioselective Synthesis of Optically Pure (R)- and (S)-β-Lysine via Nitrone Cycloaddition

Optically pure (R)- and (S)-β-lysines have been obtained via cycloaddition of chiral nitrone (4) to vinyl acetate, followed by facile chromatographic separation of the four resulting acetates (5) into two pairs of C-5 epimers and conversion of each pair i

Mechanistic Studies on Lysine 2,3-Aminomutase: Carbon-13-Deuterium Crossover Experiments

A mixture of L-lysine plus L-lysine is converted by purified lysine 2,3-aminomutase into β-lysine.The di-N-phthaloyl methyl ester derivative of the resultant β-lysine shows a geminally deuterium-coupled enriched (13)C n.m.r. signal indicating intermolecular transfer of the migrating 3-pro-R hydrogen of the α-lysine.L-Lysine has been synthesized.A mixture of L-lysine plus L-lysine is similary converted into β-lysine.Its di-N-phthaloyl methyl ester derivative shows a β-shifted enriched (13)C n.m.r. signal for C-3, but no geminally coupled enriched C-3 signal.The latter experiment rules out any intermolecular exchange of the non-migrating 3-pro-S hydrogen atom of α-lysine.Various mechanistic possibilities for the intermolecular hydrogen transfer process are discussed.