N-acetylaspartate (NAA)

Found 17 Sample Hits

m/z	Adducts	Species	Organ	Scanning	Sample
193.0836	[M+NH4]+ PPM:8.8	Posidonia oceanica	root	MALDI (CHCA)	20190614_MS1_A19r-20 - MTBLS1746 Resolution: 17μm, 262x276 Description Seagrasses are one of the most efficient natural sinks of carbon dioxide (CO2) on Earth. Despite covering less than 0.1% of coastal regions, they have the capacity to bury up to 10% of marine organic matter and can bury the same amount of carbon 35 times faster than tropical rainforests. On land, the soil’s ability to sequestrate carbon is intimately linked to microbial metabolism. Despite the growing attention to the link between plant production, microbial communities, and the carbon cycle in terrestrial ecosystems, these processes remain enigmatic in the sea. Here, we show that seagrasses excrete organic sugars, namely in the form of sucrose, into their rhizospheres. Surprisingly, the microbial communities living underneath meadows do not fully use this sugar stock in their metabolism. Instead, sucrose piles up in the sediments to mM concentrations underneath multiple types of seagrass meadows. Sediment incubation experiments show that microbial communities living underneath a meadow use sucrose at low metabolic rates. Our metagenomic analyses revealed that the distinct community of microorganisms occurring underneath meadows is limited in their ability to degrade simple sugars, which allows these compounds to persist in the environment over relatively long periods of time. Our findings reveal how seagrasses form blue carbon stocks despite the relatively small area they occupy. Unfortunately, anthropogenic disturbances are threatening the long-term persistence of seagrass meadows. Given that these sediments contain a large stock of sugars that heterotopic bacteria can degrade, it is even more important to protect these ecosystems from degradation.
193.0833	[M+NH4]+ PPM:7.3	Posidonia oceanica	root	MALDI (CHCA)	20190828_MS1_A19r-22 - MTBLS1746 Resolution: 17μm, 292x279 Description
193.0848	[M+NH4]+ PPM:15	Posidonia oceanica	root	MALDI (CHCA)	MS1_20180404_PO_1200 - MTBLS1746 Resolution: 17μm, 193x208 Description
193.0844	[M+NH4]+ PPM:13	Homo sapiens	esophagus	DESI ()	LNTO29_16_2 - MTBLS385 Resolution: 17μm, 95x101 Description
193.085	[M+NH4]+ PPM:16.1	Homo sapiens	esophagus	DESI ()	LNTO22_1_9 - MTBLS385 Resolution: 75μm, 89x74 Description
193.0843	[M+NH4]+ PPM:12.5	Homo sapiens	esophagus	DESI ()	LNTO29_16_3 - MTBLS385 Resolution: 17μm, 108x107 Description
193.0847	[M+NH4]+ PPM:14.5	Homo sapiens	esophagus	DESI ()	TO31T - MTBLS385 Resolution: 75μm, 56x54 Description
193.0849	[M+NH4]+ PPM:15.6	Homo sapiens	esophagus	DESI ()	TO29T - MTBLS385 Resolution: 75μm, 56x48 Description
193.0849	[M+NH4]+ PPM:15.6	Homo sapiens	esophagus	DESI ()	LNTO30_17_2 - MTBLS385 Resolution: 75μm, 82x54 Description
198.0339	[M+Na]+ PPM:17.1	Homo sapiens	esophagus	DESI ()	LNTO30_17_2 - MTBLS385 Resolution: 75μm, 82x54 Description
193.0845	[M+NH4]+ PPM:13.5	Homo sapiens	esophagus	DESI ()	LNTO22_1_5 - MTBLS385 Resolution: 75μm, 135x94 Description
193.0853	[M+NH4]+ PPM:17.6	Homo sapiens	esophagus	DESI ()	LNTO22_1_7 - MTBLS385 Resolution: 75μm, 69x54 Description
193.0852	[M+NH4]+ PPM:17.1	Homo sapiens	esophagus	DESI ()	LNTO22_1_8 - MTBLS385 Resolution: 75μm, 69x61 Description
198.0334	[M+Na]+ PPM:19.6	Homo sapiens	esophagus	DESI ()	LNTO22_1_8 - MTBLS385 Resolution: 75μm, 69x61 Description
193.0854	[M+NH4]+ PPM:18.1	Homo sapiens	esophagus	DESI ()	LNTO22_2_1 - MTBLS385 Resolution: 75μm, 89x88 Description
193.0844	[M+NH4]+ PPM:13	Homo sapiens	esophagus	DESI ()	LNTO29_18_2 - MTBLS385 Resolution: 75μm, 62x68 Description
193.0849	[M+NH4]+ PPM:15.6	Homo sapiens	esophagus	DESI ()	LNTO30_7_2 - MTBLS385 Resolution: 75μm, 82x68 Description

N-Acetyl-L-Aspartic acid (NAA) or N-Acetylaspartic acid, belongs to the class of organic compounds known as N-acyl-alpha amino acids. N-acyl-alpha amino acids are compounds containing an alpha amino acid which bears an acyl group at its terminal nitrogen atom. N-alpha-Acetyl-L-aspartic acid can also be classified as an alpha amino acid or a derivatized alpha amino acid. Technically, N-Acetyl-L-aspartic acid is a biologically available N-terminal capped form of the proteinogenic alpha amino acid L-aspartic acid. N-acetyl amino acids can be produced either via direct synthesis of specific N-acetyltransferases or via the proteolytic degradation of N-acetylated proteins by specific hydrolases. N-terminal acetylation of proteins is a widespread and highly conserved process in eukaryotes that is involved in protection and stability of proteins (PMID: 16465618). About 85\\\% of all human proteins and 68\\\% of all yeast proteins are acetylated at their N-terminus (PMID: 21750686). Several proteins from prokaryotes and archaea are also modified by N-terminal acetylation. The majority of eukaryotic N-terminal-acetylation reactions occur through N-acetyltransferase enzymes or NAT’s (PMID: 30054468). These enzymes consist of three main oligomeric complexes NatA, NatB, and NatC, which are composed of at least a unique catalytic subunit and one unique ribosomal anchor. The substrate specificities of different NAT enzymes are mainly determined by the identities of the first two N-terminal residues of the target protein. The human NatA complex co-translationally acetylates N-termini that bear a small amino acid (A, S, T, C, and occasionally V and G) (PMID: 30054468). NatA also exists in a monomeric state and can post-translationally acetylate acidic N-termini residues (D-, E-). NatB and NatC acetylate N-terminal methionine with further specificity determined by the identity of the second amino acid. N-acetylated amino acids, such as N-acetylaspartate can be released by an N-acylpeptide hydrolase from peptides generated by proteolytic degradation (PMID: 16465618). In addition to the NAT enzymes and protein-based acetylation, N-acetylation of free aspartic acid can also occur. In particular, N-Acetyl-L-aspartic acid can be synthesized in neurons from the amino acid aspartate and acetyl coenzyme A (acetyl CoA). Specifically, the enzyme known as aspartate N-acetyltransferase (EC 2.3.1.17) catalyzes the transfer of the acetyl group of acetyl CoA to the amino group of aspartate. N-Acetyl-L-aspartic acid is the second most concentrated molecule in the brain after the amino acid glutamate. The various functions served by N-acetylaspartic acid are still under investigation, but the primary proposed functions include (1) acting as a neuronal osmolyte that is involved in fluid balance in the brain, (2) serving as a source of acetate for lipid and myelin synthesis in oligodendrocytes (the glial cells that myelinate neuronal axons), (3) serving as a precursor for the synthesis of the important dipeptide neurotransmitter N-acetylaspartylglutamate (NAAG), and (4) playing a potential role in energy production from the amino acid glutamate in neuronal mitochondria. High neurotransmitter (i.e. N-acetylaspartic acid) levels can lead to abnormal neural signaling, delayed or arrested intellectual development, and difficulties with general motor skills. When present in sufficiently high levels, N-acetylaspartic acid can be a neurotoxin, an acidogen, and a metabotoxin. A neurotoxin is a compound that disrupts or attacks neural tissue. An acidogen is an acidic compound that induces acidosis, which has multiple adverse effects on many organ systems. A metabotoxin is an endogenously produced metabolite that causes adverse health effects at chronically high levels. Chronically high levels of N-acetylaspartic acid are associated with Canavan disease. Because N-acetylaspartic acid functions as an organic acid and high levels of organic acids can lead to a condition known... N-Acetylaspartic acid is a derivative of aspartic acid. It is the second most concentrated molecule in the brain after the amino acid glutamate. It is synthesized in neurons from the amino acid aspartate and acetyl coenzyme A. The various functions served by N-acetylaspartic acid are still under investigation, but the primary proposed functions include: Acquisition and generation of the data is financially supported in part by CREST/JST. D018377 - Neurotransmitter Agents > D018846 - Excitatory Amino Acids KEIO_ID A142 N-Acetyl-L-aspartic acid is a derivative of aspartic acid.