HUMAN ALDEHYDE DEHYDROGENASE - METABOLISM OF PUTRESCINE AND HISTAMINE

HUMAN ALDEHYDE DEHYDROGENASE - METABOLISM OF PUTRESCINE AND HISTAMINE
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DOI:
10.1111/j.1530-0277.1987.tb00167.x
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发表时间:
1987-12-01
期刊:
ALCOHOL-CLINICAL AND EXPERIMENTAL RESEARCH
影响因子:
--
通讯作者:
PIETRUSZKO, R
PIETRUSZKO, R
中科院分区:
其他
文献类型:
--
作者:
AMBROZIAK, W;PIETRUSZKO, R

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咪唑乙醛和γ-氨基丁醛、组胺和腐胺的代谢物分别是人肝醛脱氢酶(EC 1.2.1.3)胞质(E1)和线粒体(E2)同工酶的底物。在pH 7.4和500 μ M NAD下咪唑乙醛和γ-丙氨酸的Km值E1同工酶的氨基丁醛分别为40和800 μ M,E2同工酶的氨基丁醛分别为50和500 μ M。具有γ的Km值氨基丁醛与两种同工酶的Km值相对于乙醛的Km值(E1为50 μ M,E2为1 μ M)高。由于具有咪唑乙醛和γ的活性。-在纯化过程中,粗肝匀浆中的氨基丁醛与醛脱氢酶(EC 1.2.1.3)的氨基丁醛相同,似乎在人肝中该酶负责两种化合物的代谢。如果是这种情况,组胺和腐胺的代谢与酒精的代谢之间可能存在相互作用。咪唑乙醛和γ-合成了氨基丁醛,并对其稳定性进行了研究。提供了使用组胺和腐胺的合成代谢物测定醛脱氢酶的方法。
Imidazoleacetaldehyde and .gamma.-aminobutyraldehyde, metabolites of histamine and putrescine, respectively, have been shown to be substrates of human liver aldehyde dehydrogenase (EC 1.2.1.3) cytoplasmic (E1) and mitochondrial (E2) isozymes. The Km values at pH 7.4 and 500 .mu.M NAD for imidazoleacetaldehyde and .gamma.-aminobutyraldehyde for the E1 isozyme are 40 and 800 .mu.M, respectively, and for the E2 isozyme are 50 and 500 .mu.M, respectively. The Km values with .gamma.-aminobutyraldehyde with both isozymes are high relative to Km values with acetaldehyde (50 .mu.M for E1 and 1 .mu.M for E2). Since activity with both imidazoleacetaldehyde and .gamma.-aminobutyraldehyde in crude liver homogenates paralleled that of aldehyde dehydrogenase (EC 1.2.1.3) during purification it appears likely that in the human liver this enzyme is responsible for metabolism of both compounds. If this is the case, interaction between metabolism of histamine and putrescine and that of alcohol is likely. Both imidazoleacetaldehyde and .gamma.-aminobutyraldehyde were synthesized in this laboratory and their stability has been investigated. Procedures for assaying aldehyde dehydrogenase employing synthetic metabolites of histamine and putrescine are provided.