997-68-2

Basic information

• Product Name: L-SACCHAROPINE
• Synonyms: saccharopine;L-SACCHAROPINE;epsilon-N-(L-Glutar-2-yl)-L-lysine;2-[(5-amino-5-carboxy-pentyl)amino]pentanedioic acid;ε-N-(L-glutar-2-yl)-L-lysine, N6-(L-1,3-dicarboxylpropyl)-L-lysine;N-[(S)-5-Amino-5-carboxypentyl]-L-glutamic acid;(S)-2-(((S)-5-aMino-5-carboxypentyl)aMino)pentanedioic acid;N-(5-Amino-5-carboxypentyl)-L-glutamic acid
• CAS NO: 997-68-2
• Molecular Formula: C₁₁H₂₀N₂O₆
• Molecular Weight: 276.29
• Mol File: 997-68-2.mol
• Article Data: 4

Chemical Properties

• Melting Point: 257-259℃ (Decomposition)
• Boiling Point: 537.2°Cat760mmHg
• Flash Point: 278.7°C
• Appearance: /
• Density: 1.333g/cm³
• Vapor Pressure: 5.73E-13mmHg at 25°C
• Refractive Index: 1.537
• Storage Temp.: −20°C
• Solubility: Aqueous Acid (Slightly), Aqueous Base (Slightly)
• PKA: pK2 2.6; pK3 4.1; pK4 9.2; pK5 10.3(at 25℃)
• Stability: Hygroscopic
• CAS DataBase Reference: L-SACCHAROPINE(CAS DataBase Reference)
• NIST Chemistry Reference: L-SACCHAROPINE(997-68-2)
• EPA Substance Registry System: L-SACCHAROPINE(997-68-2)

Safety Data

• WGK Germany: 3
• Hazardous Substances Data: 997-68-2(Hazardous Substances Data)

Usage

Description

L-SACCHAROPINE, also known as N6-(1,3-dicarboxypropan-1-yl) derivative of L-lysine, is a compound that plays a crucial role in the metabolism of the essential amino acid lysine. It is a product of lysine breakdown and is also involved in the α-aminoadipate pathway of fungal lysine biosynthesis.

Uses

Used in Metabolic Research:
L-SACCHAROPINE is used as a biochemical marker for studying the metabolism of lysine, an essential amino acid. It helps researchers understand the metabolic pathways and mechanisms involved in lysine breakdown and its role in various physiological processes.
Used in Nutritional Studies:
L-SACCHAROPINE can be used as a nutritional supplement to support the body's lysine requirements. Lysine is an essential amino acid that plays a vital role in protein synthesis, tissue growth and repair, and the production of essential molecules like enzymes and hormones.
Used in Pharmaceutical Industry:
L-SACCHAROPINE can be used as a precursor in the synthesis of various pharmaceutical compounds. Its unique structure and properties make it a valuable building block for the development of new drugs and therapeutic agents.
Used in Fungal Lysine Biosynthesis:
L-SACCHAROPINE is used as an intermediate in the α-aminoadipate pathway of fungal lysine biosynthesis. This pathway is an alternative route for lysine production in certain fungi, and understanding its role in this process can help in the development of novel strategies for lysine production and optimization in industrial fermentation processes.

InChI:InChI=1/C11H20N2O6/c12-7(10(16)17)3-1-2-6-13-8(11(18)19)4-5-9(14)15/h7-8,13H,1-6,12H2,(H,14,15)(H,16,17)(H,18,19)/t7-,8-/m0/s1

Upstream product

• 55094-98-9 D‐α‐hydroxyglutaric acid 
• 34235-82-0 N-tosyl-N'-benzyloxycarbonyl-L-lysine 
• 55094-97-8 (S)-dimethyl 2-hydroxypentanedioate 
• 328-50-7 α-ketoglutaric acid 
• 2104-87-2 N²-(toluene-4-sulfonyl)-L-lysine 
• 56-87-1 L-lysine 
• 56-86-0 L-glutamic acid 
• 6665-12-9 L-α-aminoadipate-δ-semialdehyde 
• 64-15-3 α-ketoglutarate 

Downstream Products

• 56-87-1 L-lysine 
• 64-15-3 α-ketoglutarate 

Relevant articles and documents

Probing the chemical mechanism of saccharopine reductase from Saccharomyces cerevisiae using site-directed mutagenesis

Saccharopine reductase catalyzes the reductive amination of l-α-aminoadipate-δ-semialdehyde with l-glutamate to give saccharopine. Two mechanisms have been proposed for the reductase, one that makes use of enzyme side chains as acid-base catalytic groups, and a second, in which the reaction is catalyzed by enzyme-bound reactants. Site-directed mutagenesis was used to change acid-base candidates in the active site of the reductase to eliminate their ionizable side chain. Thus, the D126A, C154S and Y99F and several double mutant enzymes were prepared. Kinetic parameters in the direction of glutamate formation exhibited modest decreases, inconsistent with the loss of an acid-base catalyst. The pH-rate profiles obtained with all mutant enzymes decrease at low and high pH, suggesting acid and base catalytic groups are still present in all enzymes. Solvent kinetic deuterium isotope effects are all larger than those observed for wild type enzyme, and approximately equal to one another, suggesting the slow step is the same as that of wild type enzyme, a conformational change to open the site and release products (in the direction of saccharopine formation). Overall, the acid-base chemistry is likely catalyzed by bound reactants, with the exception of deprotonation of the α-amine of glutamate, which likely requires an enzyme residue.

VITAMIN COMPRISING PYROLOQUINOLINE QUINONE AND USE THEREOF

It is an object of the present invention to clarify the biochemical role of pyrroloquinoline quinone (PQQ) in living bodies by identifying an enzyme that uses PQQ as a coenzyme in mammals and then by clarifying the oxidation-reduction reaction, with which PQQ is associated as a coenzyme in living bodies. The present invention provides a method of using pyrroloquinoline quinone as a coenzyme for 2-aminoadipate 6-semialdehyde dehydrogenase.