Enzymatic N-acetylation of indolealkylamines by brain homogenates of the honeybee, Apis mellifera
Enzymatic N-acetylation of indolealkylamines by brain homogenates of the honeybee, Apis mellifera
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蜜蜂大脑匀浆对吲哚烷基胺进行酶促 N-乙酰化，Apis mellifera
DOI：
10.1016/0022-1910(75)90029-3
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发表时间：
1975
影响因子：
2.2
通讯作者：
P. Fox
中科院分区：
文献类型：
--
作者：
P. Evans;P. Fox
已发现蜜蜂（Apis mellifera）的脑匀浆具有能够催化色胺和5-羟色胺与作为乙酰基供体的乙酰辅酶A的N-乙酰化的酶。色胺N-乙酰化的Km为5.0 × 10− 7 M，pH为7.0，温度为33°C。有证据表明，吲哚烷基胺、色胺和5-羟色胺不会被单胺氧化酶（MAO）氧化，而单胺氧化酶通常被认为是脊椎动物的主要分解代谢途径。据报道，Wurtman和Axelrod的测定法对单胺氧化酶活性具有特异性，但不能区分MAO氧化和色胺N-乙酰化，因此在未仔细鉴别反应产物的情况下，不应用于测定昆虫组织中的MAO活性。吲哚酮胺的N-乙酰化的影响进行了讨论有关的神经递质的问题。
Brain homogenates of the honey-bee,Apis mellifera, have been found to possess enzymes capable of catalysing the N-acetylation of tryptamine and 5-hydroxytryptamine with acetyl coenzyme A as the acetyl donor. TheKmof the N-acetylation of tryptamine was 5·0 × 10−7M at pH 7·0 and 33°C. Evidence was obtained that the indolealkylamines, tryptamine, and 5-hydroxytryptamine, are not oxidized by monoamine oxidase (MAO) as is commonly considered to be a major catabolic route in vertebrate animals. The assay ofWurtmanandAxelrod, reportedly specific for monoamine oxidase activity, will not distinguish between oxidation by MAO and N-acetylation of tryptamine and so should not be used to assay for MAO activity in insect tissues without careful identification of the products of the reaction. Implications of N-acetylation of indoleaklamines are discussed in relation to the neurotransmitter problem.