EC Number   |
General Information |
Reference |
|---|
    2.3.1.87 | evolution |
AANAT2 evolution is mainly driven by phylogenetic relationships although catalytic properties (enzyme turnover and substrate affinity) are also under the influence of the respective species normal habitat temperature |
720470 |
| 2.3.1.87 | evolution |
evolution of insect arylalkylamine N-acetyltransferases, structural evidence from the yellow fever mosquito, Aedes aegypti, overview |
720933 |
| 2.3.1.87 | malfunction |
the abnormal Bm-iAANAT is responsible for the mln mutant, phenotype, overview. The content of dopamine in the mln mutant is about 2times higher than in the wild-type. A greater accumulation of dopamine results from the functional deficiency of Bm-iAANAT in the mutant and that the excessive dopamine is converted into dopamine melanin, causing the darker color pattern of the sclerified regions in the mln mutant compared with the wild-type |
719867 |
| 2.3.1.87 | metabolism |
arylalkylamine N-acetyltransferase is the rate-limiting enzyme of the melatonin biosynthesis pathway |
719583 |
| 2.3.1.87 | metabolism |
N-terminally acetylated Ac-AANAT is degraded through the recognition of its N-terminally acetylated N-terminal Met residue by the Ac/N-end rule pathway, whereas the non-N-terminally acetylated AANAT is targeted by the Arg/N-end rule pathway, which recognizes the unacetylated N-terminal Met-Leu sequence of rat AANAT. Degradation of Lys8Arg mutants of rat AANAT is mediated by polyubiquitylation of its Lys residue(s) |
757158 |
| 2.3.1.87 | metabolism |
serotonin N-acetyltransferase is a rate-limiting enzyme in melatonin biosynthesis in vertebrates |
720316 |
| 2.3.1.87 | metabolism |
the enzyme catalyzes the first step in melatonin biosynthesis, melatonin biosynthesis follows a 24 h day and night rhythm, which is different in fasted, fed, and refed fish, overview |
703832, 703833 |
| 2.3.1.87 | metabolism |
the enzyme catalyzes the rate-limiting step in melatonin synthesis |
705357, 705414 |
| 2.3.1.87 | metabolism |
the enzyme catalyzes the rate-limiting step in melatonin synthesis, melatonin biosynthesis pathway overview |
701705 |
| 2.3.1.87 | metabolism |
the N-terminal sequence of human AANAT differs from that of rodent AANATs. The human enzyme is longer-lived than its rat counterpart and appears to be refractory to degradation by the N-end rule pathway |
757158 |
