Characterization and kinetic analysis of indolamine N-acetyltransferase from the collaterial glands of the American cockroach, Periplaneta americana

Asano, Hironobu; Takeda, Makio

doi:10.1303/aez.33.127

Cited by 10 publications

(6 citation statements)

References 6 publications

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“…Since major neurotransmitter metabolism depends on this enzyme, it serves as an important regulator in a variety of physiological functions, metabolism, developmental determination, reproduction and behavior. Activities of aaNAT have been observed in various organs not only the CNS but also in the midgut, reproductive glands of both sexes and Malpigian tublules in the cockroach, Periplaneta americana , for example (Ichihara et al, 1997 , 2001 ; Asano and Takeda, 1998 ; Asano et al, 2003 ). Isolation and characterization of aaNAT revealed that the activities are separated to different fractions, each showing a unique optimal pH and kinetic character (Ichihara et al, 1997 , 1998 , 2001 ; Asano and Takeda, 1998 ; Sakamoto et al, 1998 ), suggesting that aaNAT activities consist of a family of enzymes.…”

Section: Historical Aspects and Reality In Insect Aanatmentioning

confidence: 99%

“…Since the enzyme employs two substrates, arylalkylamines and acetyl CoA, we made a bisubstrate kinetic analysis employing brain-SOG and collaterial gland homogenates of P. americana . The former followed ping pong Bi-Bi mechanism and the latter sequential Bi-Bi mechanism, respectively (Asano and Takeda, 1998 ; Sakamoto et al, 1998 ).…”

Section: Kinetic Aspects: How Many Enzymes?mentioning

confidence: 99%

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Structures and functions of insect arylalkylamine N-acetyltransferase (iaaNAT); a key enzyme for physiological and behavioral switch in arthropods

et al. 2015

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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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Section: Historical Aspects and Reality In Insect Aanatmentioning

confidence: 99%

Section: Kinetic Aspects: How Many Enzymes?mentioning

confidence: 99%

Structures and functions of insect arylalkylamine N-acetyltransferase (iaaNAT); a key enzyme for physiological and behavioral switch in arthropods

et al. 2015

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“…Early studies of an iAANAT from the American cockroach, Periplaneta americana . demonstrated that this enzyme functioned via a sequential kinetic mechanism (Asano and Takeda, 1998 ; Ichihara et al, 2001 ). iAANATs from other insects were purified and characterized following the work on the P. americana AANAT.…”

Section: Introductionmentioning

confidence: 99%

Insect Arylalkylamine N-Acyltransferases: Mechanism and Role in Fatty Acid Amide Biosynthesis

O’Flynn

Suarez

Hawley

et al. 2018

Front. Mol. Biosci.

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Arylalkylamine N-acyltransferases (AANATs) catalyze the formation of an N-acylamide from an acyl-CoA thioester and an amine. One well known example is the production of N-acetylserotonin from acetyl-CoA and serotonin, a reaction in the melatonin biosynthetic pathway from tryptophan. AANATs have been identified from a variety of vertebrates and invertebrates. Considerable efforts have been devoted to the mammalian AANAT because a cell-permeable inhibitor specifically targeted against this enzyme could prove useful to treat diseases related to dysfunction in melatonin production. Insects are an interesting model for the study of AANATs because more than one isoform is typically expressed by a specific insect and the different insect AANATs (iAANATs) serve different roles in the insect cell. In contrast, mammals express only one AANAT. The major role of iAANATs seem to be in the production of N-acetyldopamine, a reaction important in the tanning and sclerotization of the cuticle. Metabolites identified in insects including N-acetylserotonin and long-chain N-fatty acyl derivatives of dopamine, histidine, phenylalanine, serotonin, tyrosine, and tryptophan are likely produced by an iAANAT. In vitro studies of specific iAANATs are consistent with this hypothesis. In this review, we highlight the current metabolomic knowledge of the N-acylated aromatic amino acids and N-acylated derivatives of the aromatic amino acids, the current mechanistic understanding of the iAANATs, and explore the possibility that iAANATs serve as insect “rhymezymes” regulating photoperiodism and other rhythmic processes in insects.

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“…A broad spectrum of activities due to multiple amine substrates, different chromatographic behaviors, kinetic characteristics, and different pH dependency suggests that several NAT isoenzymes or Archives of Insect Biochemistry and Physiology different NAT genes are present in P. americana (Ichihara et al, 1997;Asano and Takeda 1998;Sakamoto et al, 1998;Asano et al, 2003). Brodbeck et al (1998), by cloning aaNAT from the abdomen of D. melanogaster, have concluded that at least two genes exist in this species.…”

Section: Introductionmentioning

confidence: 99%

Molecular cloning of a cDNA encoding arylalkylamineN-acetyltransferase from the testicular system ofPeriplaneta americana: Primary protein structure and expression analysis

Bembenek

Sakamoto

Takeda

2005

Arch. Insect Biochem. Physiol.

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DNA encoding a fragment of putative arylalkylamine N-acetyltransferase (NAT) of the American cockroach, Periplaneta americana, was amplified by PCR with degenerate primers based on the two peptides previously purified from the testicular system of this species. A full clone was obtained by RACE-PCR. The clone consisted of 89 bp 5'-UTR, 753-bp open reading frame and 712-bp 3'-UTR. The amino acid sequence of 251 residues deduced from this ORF corresponded to the predicted molecular mass of 28.5 kDa. The predicted amino acid sequence had an overall identity of 35% with NAT1 and 27% with NAT2 of Drosophila melanogaster, respectively. Structural analysis revealed that NAT from P. americana contained two motifs characteristic of the NAT superfamily and three conserved regions (C/c-1, D/c-1, D/c-2) distinguishing aaNAT subfamily. Northern blot analysis showed that the mRNA of approximately 1.5 kb was transcribed at a high level in the testicular system, and corresponded to the length of the cDNA, i.e., 1,554 bp. Significant levels of NAT transcript were also detected in the midgut, ovary and the accessory glands and at much lower levels in the fat body and brain. Southern blot analysis suggested the presence of a single copy of the cloned gene in the genome.

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Characterization and kinetic analysis of indolamine N-acetyltransferase from the collaterial glands of the American cockroach, Periplaneta americana

Cited by 10 publications

References 6 publications

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

Insect Arylalkylamine N-Acyltransferases: Mechanism and Role in Fatty Acid Amide Biosynthesis

Molecular cloning of a cDNA encoding arylalkylamineN-acetyltransferase from the testicular system ofPeriplaneta americana: Primary protein structure and expression analysis

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