Structures and functions of insect arylalkylamine N-acetyltransferase (iaaNAT); a key enzyme for physiological and behavioral switch in arthropods.
Structures and functions of insect arylalkylamine N-acetyltransferase (iaaNAT); a key enzyme for physiological and behavioral switch in arthropods.
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昆虫芳基烷基胺N-乙酰转移酶(Iaanat)的结构和功能;节肢动物中生理和行为转换的关键酶。
DOI:
10.3389/fphys.2015.00113
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发表时间:
2015
影响因子:
4
通讯作者:
Takeda M
中科院分区:
文献类型:
--
作者:
Hiragaki S;Suzuki T;Mohamed AA;Takeda M
The evolution of N-acetyltransfeases (NATs) seems complex. Vertebrate arylalkylamine N-acetyltransferase (aaNAT) has been extensively studied since it leads to the synthesis of melatonin, a multifunctional neurohormone prevalent in photoreceptor cells, and is known as a chemical token of the night. Melatonin also serves as a scavenger for reactive oxygen species. This is also true with invertebrates. NAT therefore has distinct functional implications in circadian function, as timezymes (aaNAT), and also xenobiotic reactions (arylamine NAT or simply NAT). NATs belong to a broader enzyme group, the GCN5-related N-acetyltransferase superfamily. Due to low sequence homology and a seemingly fast rate of structural differentiation, the nomenclature for NATs can be confusing. The advent of bioinformatics, however, has helped to classify this group of enzymes; vertebrates have two distinct subgroups, the timezyme type and the xenobiotic type, which has a wider substrate range including imidazolamine, pharmacological drugs, environmental toxicants and even histone. Insect aaNAT (iaaNAT) form their own clade in the phylogeny, distinct from vertebrate aaNATs. Arthropods are unique, since the phylum has exoskeleton in which quinones derived from N-acetylated monoamines function in coupling chitin and arthropodins. Monoamine oxidase (MAO) activity is limited in insects, but NAT-mediated degradation prevails. However, unexpectedly iaaNAT occurs not only among arthropods but also among basal deuterostomia, and is therefore more apomorphic. Our analyses illustrate that iaaNATs has unique physiological roles but at the same time it plays a role in a timezyme function, at least in photoperiodism. Photoperiodism has been considered as a function of circadian system but the detailed molecular mechanism is not well understood. We propose a molecular hypothesis for photoperiodism in Antheraea pernyi based on the transcription regulation of NAT interlocked by the circadian system. Therefore, the enzyme plays both unique and universal roles in insects. The unique role of iaaNATs in physiological regulation urges the targeting of this system for integrated pest management (IPM). We indeed showed a successful example of chemical compound screening with reconstituted enzyme and further attempts seem promising.
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影响因子:
1.3
作者:
Asano, H;Takeda, M
通讯作者:
Takeda, M
影响因子:
56.9
作者:
AXELROD, J
通讯作者:
AXELROD, J
DOI:
10.1016/j.cbpc.2004.03.017
发表时间:
2005-01-01
影响因子:
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作者:
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通讯作者:
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影响因子:
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作者:
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通讯作者:
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DOI:
10.1016/j.dsr.2009.06.001
发表时间:
2009-10-01
影响因子:
2.4
作者:
Aguzzi, J.;Sanchez-Pardo, J.;Sarda, F.
通讯作者:
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