L-ornithine

Base Information

• Chemical Name: L-ornithine
• CAS No.: 70-26-8
• Deprecated CAS: 7006-33-9,410523-46-5,204201-13-8
• Molecular Formula: C5H12N2O2
• Molecular Weight: 132.162
• Hs Code.: 2922499990
• European Community (EC) Number: 200-731-7
• NSC Number: 758894
• UNII: E524N2IXA3
• DSSTox Substance ID: DTXSID00883219
• Nikkaji Number: J9.177D
• Wikipedia: Ornithine
• Wikidata: Q410198
• NCI Thesaurus Code: C29611
• Pharos Ligand ID: X77237H6KSUJ
• Metabolomics Workbench ID: 37139
• ChEMBL ID: CHEMBL446143
• Mol file: 70-26-8.mol

Synonyms:2,5 Diaminopentanoic Acid;2,5-Diaminopentanoic Acid;Ornithine;Ornithine Dihydrochloride, (L)-Isomer;Ornithine Hydrochloride, (D)-Isomer;Ornithine Hydrochloride, (DL)-Isomer;Ornithine Hydrochloride, (L)-Isomer;Ornithine Monoacetate, (L)-Isomer;Ornithine Monohydrobromide, (L)-Isomer;Ornithine Monohydrochloride, (D)-Isomer;Ornithine Monohydrochloride, (DL)-Isomer;Ornithine Phosphate (1:1), (L)-Isomer;Ornithine Sulfate (1:1), (L)-Isomer;Ornithine, (D)-Isomer;Ornithine, (DL)-Isomer;Ornithine, (L)-Isomer

Chemical Property of L-ornithine

Chemical Property:

• Vapor Pressure: 1.08E-05mmHg at 25°C
• Melting Point: 140 °C
• Refractive Index: 1.4496 (estimate)
• Boiling Point: 308.718 °C at 760 mmHg
• PKA: 1.705(at 25℃)
• Flash Point: 140.508 °C
• PSA: 89.34000
• Density: 1.165 g/cm³
• LogP: 0.53780
• Storage Temp.: under inert gas (nitrogen or Argon) at 2–8 °C
• XLogP3: -4.4
• Hydrogen Bond Donor Count: 3
• Hydrogen Bond Acceptor Count: 4
• Rotatable Bond Count: 4
• Exact Mass: 132.089877630
• Heavy Atom Count: 9
• Complexity: 95

Purity/Quality:

HPLC≥98% ^*data from raw suppliers

L-Ornithine 99 ^*data from reagent suppliers

Safty Information:

• Pictogram(s): T,N
• Hazard Codes: T,N

MSDS Files:

SDS file from LookChem

Useful:

• Chemical Classes: Biological Agents -> Amino Acids and Derivatives
• Canonical SMILES: C(CC(C(=O)O)N)CN
• Isomeric SMILES: C(C[C@@H](C(=O)O)N)CN
• Recent NIPH Clinical Trials: Effect of intake of supplements containing ornithine on human health.
• Uses: Biochemical research; medicine. hepatoprotectant, anticholesteremic

Technology Process of L-ornithine

There total 128 articles about L-ornithine which guide to synthetic route it. The literature collected by LookChem mainly comes from the sharing of users and the free literature resources found by Internet computing technology. We keep the original model of the professional version of literature to make it easier and faster for users to retrieve and use. At the same time, we analyze and calculate the most feasible synthesis route with the highest yield for your reference as below:

synthetic route:

Reference yield:

C17(13)C4H18(2)H3N(15)N2O3 → 2,5-diaminopentanoic acid (70-26-8,348-66-3,616-07-9,7006-33-9,25104-12-5,410523-47-6)

Guidance literature:

C₁₇⁽¹³⁾C₄H₁₈⁽²⁾H₃N⁽¹⁵⁾N₂O₃; With palladium diacetate; In methanol; chloroform; at 0 ℃; for 0.0833333h;

at 0 ℃; for 0.666667h; Aqueous phophate buffer;

With hydrogenchloride; In water; at 140 ℃; for 5h;

Reference yield:

ethyl 2-acetamido-4-cyano-2-ethoxycarbonylbutanoate (5440-42-6) → 2,5-diaminopentanoic acid (70-26-8,348-66-3,616-07-9,7006-33-9,25104-12-5,410523-47-6)

Guidance literature:

With methanol; nickel; at 70 - 100 ℃; under 51485.6 - 58840.6 Torr; Hydrogenation_.Erhitzen des jeweils erhaltenen Reaktionsprodukts mit wss. HCl;

Reference yield:

→ 2,5-diaminopentanoic acid (70-26-8,348-66-3,616-07-9,7006-33-9,25104-12-5,410523-47-6)

Guidance literature:

With methanol; nickel; at 70 - 100 ℃; under 51485.6 - 58840.6 Torr; Hydrogenation_.Erhitzen des jeweils erhaltenen Reaktionsprodukts mit wss. HCl;

upstream raw materials:

3-aminopiperidin-2-one

D-ornithine

(R,S)-2-aminoadipic acid

D-arginine

Downstream raw materials:

3-hydroxytetrahydro-2H-pyran-2-one

5-amino-2-oxo-valeric acid

1,4-diaminobutane

1-pyrroline

Refernces

Inhibition of Aspartic Proteinases by Peptides Containing Lysine and Ornithine Side-Chain Analogues of Statine

10.1021/jm00385a010

The research focuses on the inhibition of aspartic proteinases by peptides containing lysine and ornithine side-chain analogues of statine. The purpose of this study was to design and synthesize new analogues of statine, specifically 4,8-diamino-3-hydroxyoctanoic acid ([LySta]) and 4,7-diamino-3-hydroxyheptanoic acid ([OrnSta]), based on substrate specificity and molecular modeling of three-dimensional structures. The goal was to develop selective and potent inhibitors for penicillopepsin, an aspartic proteinase. The researchers synthesized these new amino acids and used them to prepare inhibitors, measuring inhibition constants (Ki values) for their effects on porcine pepsin and penicillopepsin. The study concluded that the new inhibitors were significantly more potent against penicillopepsin than the original statine-containing inhibitor, with Ki values 10-100 times smaller, while being exceptionally weak inhibitors of porcine pepsin. The chemicals used in this process included Boc-Lys(Z)-a1, Boc-Orn(Bz1,Z)-a1, lithio ethyl acetate, trichloroethoxycarbonyl derivatives, and various other reagents and solvents for peptide synthesis and purification.

Side chain modified 5-deazafolate and 5-deazatetrahydrofolate analogues as mammalian folylpolyglutamate synthetase and glycinamide ribonucleotide formyltransferase inhibitors: Synthesis and in vitro biological evaluation

10.1021/jm00087a012

This research aimed to synthesize and evaluate a series of 5-deazafolate and 5-deazatetrahydrofolate analogues as potential inhibitors of folylpolyglutamate synthetase (FPGS) and glycinamide ribonucleotide formyltransferase (GARFT), enzymes involved in folate metabolism and purine biosynthesis, respectively. The researchers synthesized analogues by replacing the glutamic acid side chain with homocysteic acid (HCysA), 2-amino-4-phosphonobutanoic acid (APBA), and ornithine (Om). The compounds were tested for their inhibitory effects on mouse liver FPGS and GARFT. The results showed that the analogues with HCysA and monoethyl APBA side chains were less active as FPGS inhibitors, while Orn and APBA analogues exhibited competitive inhibition kinetics and were more potent, with Ki values as low as 30 nM.