人类单胺氧化酶A和B基因具有相同的外显子-内含子结构。
Human monoamine oxidase A and B genes exhibit identical exon-intron organization.
作者信息
Grimsby J, Chen K, Wang L J, Lan N C, Shih J C
机构信息
Department of Molecular Pharmacology and Toxicology, School of Pharmacy, University of Southern California, Los Angeles 90033.
出版信息
Proc Natl Acad Sci U S A. 1991 May 1;88(9):3637-41. doi: 10.1073/pnas.88.9.3637.
Abstract
Monoamine oxidases A and B [MAOA and MAOB; amine:oxygen oxidoreductase (deaminating) (flavin-containing), EC 1.4.3.4] play important roles in the metabolism of neuroactive, vasoactive amines and the Parkinsonism-producing neurotoxin 1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine (MPTP). Human MAOA and MAOB genes isolated from X chromosome-specific libraries span at least 60 kilobases, consist of 15 exons, and exhibit identical exon-intron organization. Exon 12 codes for the covalent FAD-binding-site and is the most conserved exon; the MAOA and MAOB exon 12 products share 93.9% peptide identity. These results suggest that MAOA and MAOB are derived from duplication of a common ancestral gene and provide insight on the structural/functional relationship of the enzyme products.
摘要
单胺氧化酶A和B [MAOA和MAOB；胺：氧氧化还原酶（脱氨基）（含黄素），EC 1.4.3.4] 在神经活性、血管活性胺以及导致帕金森症的神经毒素1-甲基-4-苯基-1,2,3,6-四氢吡啶（MPTP）的代谢中发挥重要作用。从X染色体特异性文库中分离出的人类MAOA和MAOB基因跨度至少60千碱基，由15个外显子组成，并呈现出相同的外显子-内含子结构。外显子12编码共价FAD结合位点，是最保守的外显子；MAOA和MAOB外显子12的产物具有93.9%的肽同一性。这些结果表明，MAOA和MAOB源自一个共同祖先基因的复制，并为酶产物的结构/功能关系提供了见解。
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