Bovine Metabolome Database: Showing metabocard for N-Methyl-D-aspartic acid (BMDB0002393)

Identification Taxonomy Physical properties Pathways Spectra Concentrations Links References enzymes (9) Show 9 proteins XML

Record Information

Version

1.0

Creation Date

2016-09-30 22:55:01 UTC

Update Date

2020-05-11 20:30:37 UTC

BMDB ID

BMDB0002393

Secondary Accession Numbers

BMDB02393

Metabolite Identification

Common Name

N-Methyl-D-aspartic acid

Description

N-Methyl-D-aspartic acid, also known as N-methylaspartate or (R)-2-methylamino-succinate, belongs to the class of organic compounds known as aspartic acid and derivatives. Aspartic acid and derivatives are compounds containing an aspartic acid or a derivative thereof resulting from reaction of aspartic acid at the amino group or the carboxy group, or from the replacement of any hydrogen of glycine by a heteroatom. N-Methyl-D-aspartic acid exists as a solid, possibly soluble (in water), and a very strong basic compound (based on its pKa) molecule.

Structure

MOL SDF 3D-SDF PDB SMILES InChI View 3D Structure

Synonyms

Value	Source
(R)-2-Methylamino-succinic acid	ChEBI
2-Methylamino-succinic acid	ChEBI
Methyl aspartic acid	ChEBI
N-Methyl aspartic acid	ChEBI
N-Methyl-D-aspartate	ChEBI
N-Methylaspartate	ChEBI
NMDA	ChEBI
(R)-2-Methylamino-succinate	Generator
2-Methylamino-succinate	Generator
Methyl aspartate	Generator
N-Methyl aspartate	Generator
N-Methylaspartic acid	Generator
Acid, N-methyl-D-aspartic	MeSH
N Methyl D aspartate	MeSH
N Methyl D aspartic acid	MeSH
N Methylaspartate	MeSH
N-Me-D-asp-OH	HMDB
N-Methyl D-aspartate	HMDB
N-Methyl D-aspartic acid	HMDB

Chemical Formula

C₅H₉NO₄

Average Molecular Weight

147.1293

Monoisotopic Molecular Weight

147.053157781

IUPAC Name

(2R)-2-(methylamino)butanedioic acid

Traditional Name

N methyl D aspartate

CAS Registry Number

6384-92-5

SMILES

CN[C@H](CC(O)=O)C(O)=O

InChI Identifier

InChI=1S/C5H9NO4/c1-6-3(5(9)10)2-4(7)8/h3,6H,2H2,1H3,(H,7,8)(H,9,10)/t3-/m1/s1

InChI Key

HOKKHZGPKSLGJE-GSVOUGTGSA-N

Chemical Taxonomy

Description

belongs to the class of organic compounds known as aspartic acid and derivatives. Aspartic acid and derivatives are compounds containing an aspartic acid or a derivative thereof resulting from reaction of aspartic acid at the amino group or the carboxy group, or from the replacement of any hydrogen of glycine by a heteroatom.

Kingdom

Organic compounds

Super Class

Organic acids and derivatives

Class

Carboxylic acids and derivatives

Sub Class

Amino acids, peptides, and analogues

Direct Parent

Aspartic acid and derivatives

Alternative Parents

Substituents

Aspartic acid or derivatives
Alpha-amino acid
D-alpha-amino acid
Dicarboxylic acid or derivatives
Fatty acid
Amino acid
Carboxylic acid
Secondary aliphatic amine
Secondary amine
Amine
Organooxygen compound
Organonitrogen compound
Organic oxygen compound
Organic nitrogen compound
Carbonyl group
Organopnictogen compound
Organic oxide
Hydrocarbon derivative
Aliphatic acyclic compound

Molecular Framework

Aliphatic acyclic compounds

External Descriptors

secondary amino compound (CHEBI:31882 )
amino dicarboxylic acid (CHEBI:31882 )
D-alpha-amino acid (CHEBI:31882 )
D-aspartic acid derivative (CHEBI:31882 )

Ontology

Status

Detected but not Quantified

Origin

Not Available

Biofunction

Not Available

Application

Not Available

Cellular locations

Cytoplasm

Physical Properties

State

Solid

Experimental Properties

Property	Value	Reference
Melting Point	187 - 192 °C	Not Available
Boiling Point	Not Available	Not Available
Water Solubility	Not Available	Not Available
LogP	Not Available	Not Available

Predicted Properties

Property	Value	Source
logP	-2.6	ALOGPS
logP	-3.3	ChemAxon
logS	-0.56	ALOGPS
pKa (Strongest Acidic)	1.46	ChemAxon
pKa (Strongest Basic)	10.34	ChemAxon
Physiological Charge	-1	ChemAxon
Hydrogen Acceptor Count	5	ChemAxon
Hydrogen Donor Count	3	ChemAxon
Polar Surface Area	86.63 Å²	ChemAxon
Rotatable Bond Count	4	ChemAxon
Refractivity	31.31 m³·mol⁻¹	ChemAxon
Polarizability	13.18 Å³	ChemAxon
Number of Rings	0	ChemAxon
Bioavailability	Yes	ChemAxon
Rule of Five	Yes	ChemAxon
Ghose Filter	Yes	ChemAxon
Veber's Rule	Yes	ChemAxon
MDDR-like Rule	Yes	ChemAxon

Spectra

Biological Properties

Cellular Locations

Cytoplasm

Biospecimen Locations

Brain
Fibroblasts
Kidney
Milk
Neuron

Pathways

Not Available

Name	SMPDB/Pathwhiz	KEGG

Normal Concentrations

Biospecimen	Status	Value	Age	Sex	Condition	Reference	Details
Brain	Expected but not Quantified	Not Quantified	Not Specified	Not Specified	Normal	Not Applicable	details
Fibroblasts	Expected but not Quantified	Not Quantified	Not Specified	Not Specified	Normal	Not Applicable	details
Kidney	Expected but not Quantified	Not Quantified	Not Specified	Not Specified	Normal	Not Applicable	details
Milk	Detected but not Quantified	Not Quantified	Not Specified	Not Specified	Normal	PMID: 28306241	details
Neuron	Expected but not Quantified	Not Quantified	Not Specified	Not Specified	Normal	Not Applicable	details

Abnormal Concentrations

Not Available

External Links

HMDB ID

HMDB0002393

DrugBank ID

Not Available

Phenol Explorer Compound ID

Not Available

FooDB ID

FDB022992

KNApSAcK ID

Not Available

Chemspider ID

21436

KEGG Compound ID

C12269

BioCyc ID

CPD-10705

BiGG ID

Not Available

Wikipedia Link

N-Methyl-D-aspartic_acid

METLIN ID

6662

PubChem Compound

22880

PDB ID

Not Available

ChEBI ID

31882

References

Synthesis Reference

Not Available

Material Safety Data Sheet (MSDS)

Not Available

General References

Mung D, Li L: Development of Chemical Isotope Labeling LC-MS for Milk Metabolomics: Comprehensive and Quantitative Profiling of the Amine/Phenol Submetabolome. Anal Chem. 2017 Apr 18;89(8):4435-4443. doi: 10.1021/acs.analchem.6b03737. Epub 2017 Mar 28. [PubMed:28306241 ]

Enzymes

Enzyme Details

1. Platelet-activating factor acetylhydrolase IB subunit alpha

General function:: Involved in dynactin binding
Specific function:: Positively regulates the activity of the minus-end directed microtubule motor protein dynein. May enhance dynein-mediated microtubule sliding by targeting dynein to the microtubule plus end. Required for several dynein- and microtubule-dependent processes such as the maintenance of Golgi integrity, the peripheral transport of microtubule fragments and the coupling of the nucleus and centrosome. Required during brain development for the proliferation of neuronal precursors and the migration of newly formed neurons from the ventricular/subventricular zone toward the cortical plate. Neuronal migration involves a process called nucleokinesis, whereby migrating cells extend an anterior process into which the nucleus subsequently translocates. During nucleokinesis dynein at the nuclear surface may translocate the nucleus towards the centrosome by exerting force on centrosomal microtubules. Also required for proper activation of Rho GTPases and actin polymerization at the leading edge of locomoting cerebellar neurons and postmigratory hippocampal neurons in response to calcium influx triggered via NMDA receptors. May also play a role in other forms of cell locomotion including the migration of fibroblasts during wound healing (By similarity). Non-catalytic subunit of an acetylhydrolase complex which inactivates platelet-activating factor (PAF) by removing the acetyl group at the SN-2 position. Required for pronuclear migration during fertilization. Required for dynein recruitment to microtubule plus ends and BICD2-bound cargos (By similarity).
Gene Name:: PAFAH1B1
Uniprot ID:: P43033
Molecular weight:: 46613.0

Enzyme Details

2. Solute carrier family 22 member 1

General function:: Carbohydrate transport and metabolism
Specific function:: Translocates a broad array of organic cations with various structures and molecular weights including the model compounds 1-methyl-4-phenylpyridinium (MPP), tetraethylammonium (TEA), N-1-methylnicotinamide (NMN), 4-(4-(dimethylamino)styryl)-N-methylpyridinium (ASP), the endogenous compounds choline, guanidine, histamine, epinephrine, adrenaline, noradrenaline and dopamine, and the drugs quinine, and metformin. The transport of organic cations is inhibited by a broad array of compounds like tetramethylammonium (TMA), cocaine, lidocaine, NMDA receptor antagonists, atropine, prazosin, cimetidine, TEA and NMN, guanidine, cimetidine, choline, procainamide, quinine, tetrabutylammonium, and tetrapentylammonium. Translocates organic cations in an electrogenic and pH-independent manner. Translocates organic cations across the plasma membrane in both directions. Transports the polyamines spermine and spermidine. Transports pramipexole across the basolateral membrane of the proximal tubular epithelial cells. The choline transport is activated by MMTS. Regulated by various intracellular signaling pathways including inhibition by protein kinase A activation, and endogenously activation by the calmodulin complex, the calmodulin-dependent kinase II and LCK tyrosine kinase (By similarity).
Gene Name:: SLC22A1
Uniprot ID:: A7MBE0
Molecular weight:: 62502.0

Enzyme Details

3. Calcium-binding protein 1

General function:: Involved in calcium ion binding
Specific function:: Modulates calcium-dependent activity of inositol 1,4,5-triphosphate receptors (ITPRs). Inhibits agonist-induced intracellular calcium signaling. Enhances inactivation and does not support calcium-dependent facilitation of voltage-dependent P/Q-type calcium channels. Causes calcium-dependent facilitation and inhibits inactivation of L-type calcium channels by binding to the same sites as calmodulin in the C-terminal domain of CACNA1C, but has an opposite effect on channel function. Suppresses the calcium-dependent inactivation of CACNA1D. Inhibits TRPC5 channels. Prevents NMDA receptor-induced cellular degeneration. Required for the normal transfer of light signals through the retina.
Gene Name:: CABP1
Uniprot ID:: Q9N1R0
Molecular weight:: 25755.0

Enzyme Details

4. Little elongation complex subunit 2

General function:: Not Available
Specific function:: Component of the little elongation complex (LEC), a complex required to regulate small nuclear RNA (snRNA) gene transcription by RNA polymerase II and III.
Gene Name:: ICE2
Uniprot ID:: Q0VCQ7
Molecular weight:: 109914.0

Enzyme Details

5. Protein lifeguard 1

General function:: Not Available
Specific function:: Potential apoptotic regulator.
Gene Name:: GRINA
Uniprot ID:: Q32L53
Molecular weight:: 40232.0

Enzyme Details

6. Protein lin-7 homolog C

General function:: Involved in exocytosis
Specific function:: Plays a role in establishing and maintaining the asymmetric distribution of channels and receptors at the plasma membrane of polarized cells. Forms membrane-associated multiprotein complexes that may regulate delivery and recycling of proteins to the correct membrane domains. The tripartite complex composed of LIN7 (LIN7A, LIN7B or LIN7C), CASK and APBA1 may have the potential to couple synaptic vesicle exocytosis to cell adhesion in brain. Ensures the proper localization of GRIN2B (subunit 2B of the NMDA receptor) to neuronal postsynaptic density and may function in localizing synaptic vesicles at synapses where it is recruited by beta-catenin and cadherin. Required to localize Kir2 channels, GABA transporter (SLC6A12) and EGFR/ERBB1, ERBB2, ERBB3 and ERBB4 to the basolateral membrane of epithelial cells (By similarity).
Gene Name:: LIN7C
Uniprot ID:: Q0P5F3
Molecular weight:: 21834.0

Enzyme Details

7. Protein lin-7 homolog B

General function:: Involved in protein binding
Specific function:: Plays a role in establishing and maintaining the asymmetric distribution of channels and receptors at the plasma membrane of polarized cells. Forms membrane-associated multiprotein complexes that may regulate delivery and recycling of proteins to the correct membrane domains. The tripartite complex composed of LIN7 (LIN7A, LIN7B or LIN7C), CASK and APBA1 may have the potential to couple synaptic vesicle exocytosis to cell adhesion in brain. Ensures the proper localization of GRIN2B (subunit 2B of the NMDA receptor) to neuronal postsynaptic density and may function in localizing synaptic vesicles at synapses where it is recruited by beta-catenin and cadherin. Required to localize Kir2 channels, GABA transporter (SLC6A12) and EGFR/ERBB1, ERBB2, ERBB3 and ERBB4 to the basolateral membrane of epithelial cells. May increase the amplitude of ASIC3 acid-evoked currents by stabilizing the channel at the cell surface (By similarity).
Gene Name:: LIN7B
Uniprot ID:: Q2KIB6
Molecular weight:: 22280.0

Enzyme Details

8. Protein lin-7 homolog A

General function:: Involved in protein binding
Specific function:: Plays a role in establishing and maintaining the asymmetric distribution of channels and receptors at the plasma membrane of polarized cells. Forms membrane-associated multiprotein complexes that may regulate delivery and recycling of proteins to the correct membrane domains. The tripartite complex composed of LIN7 (LIN7A, LIN7B or LIN7C), CASK and APBA1 may have the potential to couple synaptic vesicle exocytosis to cell adhesion in brain. Ensures the proper localization of GRIN2B (subunit 2B of the NMDA receptor) to neuronal postsynaptic density and may function in localizing synaptic vesicles at synapses where it is recruited by beta-catenin and cadherin. Required to localize Kir2 channels, GABA transporter (SLC6A12) and EGFR/ERBB1, ERBB2, ERBB3 and ERBB4 to the basolateral membrane of epithelial cells (By similarity).
Gene Name:: LIN7A
Uniprot ID:: Q32LM6
Molecular weight:: 25997.0

Enzyme Details

9. Sodium- and chloride-dependent glycine transporter 1

General function:: Involved in neurotransmitter:sodium symporter activity
Specific function:: Terminates the action of glycine by its high affinity sodium-dependent reuptake into presynaptic terminals. May play a role in regulation of glycine levels in NMDA receptor-mediated neurotransmission (By similarity).
Gene Name:: SLC6A9
Uniprot ID:: Q28039
Molecular weight:: 71318.0

Showing metabocard for N-Methyl-D-aspartic acid (BMDB0002393)

Structure for BMDB0002393 (N-Methyl-D-aspartic acid)

Enzymes