3038-89-9

Basic information

• Product Name: delta-1-piperidine-6-carboxylic acid
• Synonyms: delta-1-piperidine-6-carboxylic acid;2-Pyridinecarboxylic acid, 2,3,4,5-tetrahydro-;2,3,4,5-tetrahydropyridine-2-carb. Acid;1-piperideine-6-carboxylic acid
• CAS NO: 3038-89-9
• Molecular Formula: C₆H₉NO₂
• Molecular Weight: 127.14116
• Mol File: 3038-89-9.mol
• Article Data: 3

Chemical Properties

• Boiling Point: 309°Cat760mmHg
• Flash Point: 140.7°C
• Appearance: /
• Density: 1.27g/cm³
• Vapor Pressure: 0.000147mmHg at 25°C
• PKA: 2.53±0.20(Predicted)
• CAS DataBase Reference: delta-1-piperidine-6-carboxylic acid(CAS DataBase Reference)
• NIST Chemistry Reference: delta-1-piperidine-6-carboxylic acid(3038-89-9)
• EPA Substance Registry System: delta-1-piperidine-6-carboxylic acid(3038-89-9)

Safety Data

• Hazardous Substances Data: 3038-89-9(Hazardous Substances Data)

Usage

Definition

ChEBI: A tetrahydropyridine that is 2,3,4,5-tetrahydropyridine having a carboxy group at the 2-position.

InChI:InChI=1/C6H9NO2/c8-6(9)5-3-1-2-4-7-5/h4-5H,1-3H2,(H,8,9)/p-1

Upstream product

• 56-87-1 L-lysine 
• 4043-87-2 pipecolic Acid 

Downstream Products

• 27300-27-2 1-(3,4,5,6-tetrahydro-2-pyridyl)-1-ethanone 

Relevant articles and documents

First crystal structure of L-lysine 6-dehydrogenase as an NAD-dependent amine dehydrogenase

A gene encoding an L-lysine dehydrogenase was identified in the hyperthermophilic archaeon Pyrococcus horikoshii. The gene was overexpressed in Escherichia coli, and its product was purified and characterized. The expressed enzyme is the most thermostable L-lysine dehydrogenase yet described, with a half-life of 180 min at 100 °C. The product of the enzyme's catalytic activity is Δ1-piperideine-6-carboxylate, which makes this enzyme an L-lysine 6-dehydrogenase (EC 1.4.1.18) that catalyzes the reductive deamination of the ∈-amino group and a type of NAD-dependent amine dehydrogenase. The three-dimensional structure of the enzyme was determined using the mercury-based multiple-wavelength anomalous dispersion method at a resolution of 2.44 A in the presence of NAD and sulfate ion. The asymmetric unit consisted of two subunits, and a crystallographic 2-fold axis generated the functional dimer. Each monomer consisted of a Rossmann fold domain and a C-terminal catalytic domain, and the fold of the catalytic domain showed similarity to that of saccharopine reductase. Notably, the structures of subunits A and B differed significantly. In subunit A, the active site contained a sulfate ion that was not seen in subunit B. Consequently, subunit A adopted a closed conformation, whereas subunit B adopted an open one. In each subunit, one NAD molecule was bound to the active site in an anti-conformation, indicating that the enzyme makes use of pro-R-specific hydride transfer between the two hydrides at C-4 of NADH (type A specificity). This is the first description of the three-dimensional structure of L-lysine 6-dehydrogenase as an NAD-dependent amine dehydrogenase.

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.