THE IRREVERSIBLE INACTIVATION OF 2 COPPER-DEPENDENT MONOOXYGENASES BY SULFITE - PEPTIDYLGLYCINE ALPHA-AMIDATING ENZYME AND DOPAMINE BETA-MONOOXYGENASE

被引：14

作者：

MERKLER, DJ

KULATHILA, R

FRANCISCO, WA

ASH, DE

BELL, J

机构：

[1] UNIV CALIF BERKELEY,DEPT CHEM,BERKELEY,CA 94720

[2] TEMPLE UNIV,SCH MED,DEPT BIOCHEM,PHILADELPHIA,PA 19140

来源：

FEBS LETTERS | 1995年 / 366卷 / 2-3期

关键词：

SULFITE-MEDIATED INACTIVATION; PEPTIDE ALPHA-AMIDATION; DOPAMINE HYDROXYLATION; COPPER-DEPENDENT MONOOXYGENASE;

D O I：

10.1016/0014-5793(95)00516-C

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Peptidylglycine alpha-amidating enzyme (alpha-AE) and dopamine beta-monooxygenase (D beta M), two copper-dependent monooxygenases that have catalytic and structural similarities, are irreversibly inactivated by sodium sulfite in a time- and concentration-dependent manner. Studies with alpha-AE show that the sulfite-mediated inactivation is dependent on the presence of redox active transition metals free in solution, with Cu(II) being the mast effective in supporting the inactivation reaction. Sulfite inactivation of alpha-AE is specific for the monooxygenase reaction of this bifunctional enzyme and amidated peptides provide protection against the inactivation. Consequently, the sulfite-mediated inactivation of alpha-AE and D beta M most likely results from the transition metal-catalyzed oxidation of sulfite to the sulfite radical, SO3-.

引用

页码：165 / 169

页数：5

共 35 条

[1] CHEMICAL MODIFICATION OF RHODANESE WITH SULFITE [J].