2022
DOI: 10.1007/s00253-022-12028-4
|View full text |Cite
|
Sign up to set email alerts
|

Aromatic L-amino acid decarboxylases: mechanistic features and microbial applications

Help me understand this report

Search citation statements

Order By: Relevance

Paper Sections

Select...
3
1
1

Citation Types

0
4
0

Year Published

2023
2023
2024
2024

Publication Types

Select...
8
1

Relationship

0
9

Authors

Journals

citations
Cited by 16 publications
(7 citation statements)
references
References 103 publications
0
4
0
Order By: Relevance
“…Finally, GO and KEGG enrichment analyses revealed the importance of two common DEGs, AADC and AGXT2. AADCs are homologous pyridoxal-5 ′ -phosphate (PLP, active form of vitamin B6)-dependent enzymes that catalyze the conversion of aromatic L-amino acids into aromatic monoamines, mainly including the neurotransmitters dopamine, serotonin, and tyramine [26,27]. The accumulation of neurotransmitters causes overactivation of neurons, leaving the individual in a constant state of excitement, and even has a toxic effect on individual health.…”
Section: Discussionmentioning
confidence: 99%
“…Finally, GO and KEGG enrichment analyses revealed the importance of two common DEGs, AADC and AGXT2. AADCs are homologous pyridoxal-5 ′ -phosphate (PLP, active form of vitamin B6)-dependent enzymes that catalyze the conversion of aromatic L-amino acids into aromatic monoamines, mainly including the neurotransmitters dopamine, serotonin, and tyramine [26,27]. The accumulation of neurotransmitters causes overactivation of neurons, leaving the individual in a constant state of excitement, and even has a toxic effect on individual health.…”
Section: Discussionmentioning
confidence: 99%
“…It was reported that, in mammals, phenylalanine can be metabolized by phenylalanine hydroxylase, and such enzymatic activities were also established in bacteria and lower eukaryote organisms [55]. Additionally, the differences in phenylalanine concentration in non-fermented bovine colostrum can be explained by the possible different effectiveness of its conversion to tyrosine [56] and, in fermented samples, the differences in phenylalanine concentration may be attained due to the distinct activities of microbial decarboxylase, which leads to different phenylalanine conversion to phenylethylamine [57]. -control group samples; -samples fermented with Lp.…”
Section: Phenylalanine Contentmentioning
confidence: 99%
“…Phytomelatonin biosynthesis involves four main synthetic routes, all of which require tryptophan as the initial substrate and at least six enzymes, namely tryptophan decarboxylase (TDC), tryptophan hydroxylase (TPH), tryptamine 5-hydroxylase (T5H), serotonin N-acetyltransferase (SNAT), N-acetylserotonin methyltransferase (ASMT), and caffeic-O-methyltransferase (COMT) [8,9]. Among these enzymes, TDC belongs to a group of aromatic-L-amino acid decarboxylases (AADCs), which catalyze the conversion of aromatic L-amino acids to aromatic monoamines and play a crucial role in the synthesis of secondary metabolites in plants [10]. Two important AADCs in plants are TDC and tyrosine decarboxylase (TyrDC) [11], of which TDC uses tryptophan as a substrate, whereas TyrDC uses tyrosine, but both enzymes are involved in the synthesis of various alkaloid metabolites [10,12].…”
Section: Introductionmentioning
confidence: 99%
“…Among these enzymes, TDC belongs to a group of aromatic-L-amino acid decarboxylases (AADCs), which catalyze the conversion of aromatic L-amino acids to aromatic monoamines and play a crucial role in the synthesis of secondary metabolites in plants [10]. Two important AADCs in plants are TDC and tyrosine decarboxylase (TyrDC) [11], of which TDC uses tryptophan as a substrate, whereas TyrDC uses tyrosine, but both enzymes are involved in the synthesis of various alkaloid metabolites [10,12]. Additionally, TDC is responsible for catalyzing the rate-limiting reaction during the synthesis of melatonin.…”
Section: Introductionmentioning
confidence: 99%