N-Acetyltryptophan

Found 12 Sample Hits

m/z	Adducts	Species	Organ	Scanning	Sample
285.1962	[M+K]+ PPM:7	Vitis vinifera	Fruit	MALDI (DHB)	grape_dhb_91_1 - Grape Database Resolution: 50μm, 120x114 Description Grape berries fruit, condition: Ripe
285.196	[M+K]+ PPM:7.7	Vitis vinifera	Fruit	MALDI (DHB)	grape_dhb_164_1 - Grape Database Resolution: 17μm, 136x122 Description Grape berries fruit, condition: Late
285.1962	[M+K]+ PPM:7	Vitis vinifera	Fruit	MALDI (DHB)	grape_dhb_163_1 - Grape Database Resolution: 17μm, 132x115 Description Grape berries fruit, condition: Late
247.1106	[M+H]+ PPM:11.7	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.
285.1957	[M+K]+ PPM:8.7	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.
229.1014	[M+H-H2O]+ PPM:18.6	Posidonia oceanica	root	MALDI (CHCA)	20190613_MS1_A19r-18 - MTBLS1746 Resolution: 17μm, 246x264 Description
247.1116	[M+H]+ PPM:15.7	Posidonia oceanica	root	MALDI (CHCA)	20190613_MS1_A19r-18 - MTBLS1746 Resolution: 17μm, 246x264 Description
264.1345	[M+NH4]+ PPM:0.9	Posidonia oceanica	root	MALDI (CHCA)	20190613_MS1_A19r-18 - MTBLS1746 Resolution: 17μm, 246x264 Description
285.1962	[M+K]+ PPM:7	Posidonia oceanica	root	MALDI (CHCA)	20190613_MS1_A19r-18 - MTBLS1746 Resolution: 17μm, 246x264 Description
247.1114	[M+H]+ PPM:14.9	Posidonia oceanica	root	MALDI (CHCA)	MS1_20180404_PO_1200 - MTBLS1746 Resolution: 17μm, 193x208 Description
246.125	[M-H2O+NH4]+ PPM:5.3	Homo sapiens	esophagus	DESI ()	LNTO22_1_4 - MTBLS385 Resolution: 17μm, 82x80 Description
247.108	[M+H]+ PPM:1.2	Homo sapiens	esophagus	DESI ()	LNTO22_1_4 - MTBLS385 Resolution: 17μm, 82x80 Description

N-Acetyl-L-tryptophan or N-Acetyltryptophan, 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-Acetyltryptophan can also be classified as an alpha amino acid or a derivatized alpha amino acid. Technically, N-Acetyltryptophan is a biologically available N-terminal capped form of the proteinogenic alpha amino acid L-tryptophan. 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-acetyltryptophan 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 tryptophan can also occur. Many N-acetylamino acids, including N-acetyltryptophan are classified as uremic toxins if present in high abundance in the serum or plasma (PMID: 26317986; PMID: 20613759). Uremic toxins are a diverse group of endogenously produced molecules that, if not properly cleared or eliminated by the kidneys, can cause kidney damage, cardiovascular disease and neurological deficits (PMID: 18287557). N-Acetyltryptophan has also been used as a protein stabilizer. It prevents protein molecules from oxidative degradation by scavenging oxygen dissolved in protein solutions (PMID: 21903216 ). N-Acetyltryptophan has been identified as a catabolite of tryptophan generated by the gut microbiota. After absorption through the intestinal epithelium, tryptophan catabolites enter the bloodstream and are later excreted in the urine (PMID: 28916042). N-Acetyltryptophan is an inhibitor of cytochrome c release and an antagonist of the neurokinin 1 receptor (NK-1R). These inhibitory effects are thought have a useful role in neuroprotection. For instance, in mouse models of amyotrophic lateral sclerosis (ALS) the administration of N-Acetyltryptophan has been shown delay disease onset, extend survival, and ameliorate deterioration in motor performance ALS transgenic mice (PMID: 25986728). N-acetyltryptophan has been shown to significantly reduce blood-brain barrier permeability and improve functional outcome in rat models of traumatic brain injury (PMID: 29256408). N-Acetyltryptophan has also been shown to have a role in preventing hepatic ischemia-reperfusion injury. This is thought to occur through de-activation of the RIP2/caspase/IL-1beta signaling pathway (PMID: 31184936). D004791 - Enzyme Inhibitors > D011480 - Protease Inhibitors Ac-DL-Trp-OH is an endogenous metabolite. Ac-DL-Trp-OH is an endogenous metabolite. N-Acetyl-L-tryptophan is an endogenous metabolite.