A highly conserved active site helix present within the P-450 superfamily of proteins is found also in monoamine oxidase (MAO) B, a major enzyme that catalyzes deamination of neuro- and vaso-active amines in the nervous system of mammals. Mutation within the conserved region of the MAO B enzyme directly reduces MAO B's activity and alters its pH profile, which allows for indirect regulation of the cellular neurotransmitters and vasoamines.
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机译:在单胺氧化酶(MAO)B中也发现了存在于蛋白质P-450超家族中的高度保守的活性位点螺旋,MAO B是催化哺乳动物神经系统中神经和血管活性胺脱氨的主要酶。 MAO B酶保守区内的突变会直接降低MAO B的活性并改变其pH值,从而可以间接调节细胞神经递质和血管胺。
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