HUMAN MONOAMINE OXIDASE-A AND OXIDASE-B GENES EXHIBIT IDENTICAL EXON INTRON ORGANIZATION

被引:234
作者
GRIMSBY, J [1 ]
CHEN, K [1 ]
WANG, LJ [1 ]
LAN, NC [1 ]
SHIH, JC [1 ]
机构
[1] UNIV SO CALIF,SCH PHARM,DEPT MOLEC PHARMAC & TOXICOL,1985 ZONAL AVE,LOS ANGELES,CA 90033
关键词
HUMAN MAOA AND MAOB GENES; GENOMIC ORGANIZATION;
D O I
10.1073/pnas.88.9.3637
中图分类号
O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];
学科分类号
07 ; 0710 ; 09 ;
摘要
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.
引用
收藏
页码:3637 / 3641
页数:5
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