Chemical aspects of amine oxidation by flavoprotein enzymes

被引：76

作者：

Scrutton, NS ^{[1
]}

机构：

[1] Univ Leicester, Dept Biochem, Leicester LE1 7RH, Leics, England

来源：

NATURAL PRODUCT REPORTS | 2004年 / 21卷 / 06期

关键词：

D O I：

10.1039/b306788m

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：

The mechanism of amine oxidation by flavoprotein enzymes is critically analysed through analysis of available experimental data. The review assesses available evidence for radical and polar mechanisms, drawing on data from model reactions, kinetic and spectroscopic approaches, structural and mutagenesis studies. The review focuses on studies of mammalian monoamine oxidases and the bacterial enzymes trimethylamine dehydrogenase, monomeric sarcosine oxidase and dimethylglycine oxidase.

引用

页码：722 / 730

页数：9

共 117 条

[1] Vibrationally enhanced hydrogen tunneling in the Escherichia coli thymidylate synthase catalyzed reaction [J].

Agrawal, N ;

Hong, BY ;

Mihai, C ;

Kohen, A .

BIOCHEMISTRY, 2004, 43 (07) :1998-2006

[2] Barrier passage and protein dynamics in enzymatically catalyzed reactions [J].

Antoniou, D ;

Caratzoulas, S ;

Kalyanaraman, C ;

Mincer, JS ;

Schwartz, SD .

EUROPEAN JOURNAL OF BIOCHEMISTRY, 2002, 269 (13) :3103-3112

[3] UNMASKING OF HYDROGEN TUNNELING IN THE HORSE LIVER ALCOHOL-DEHYDROGENASE REACTION BY SITE-DIRECTED MUTAGENESIS [J].

BAHNSON, BJ ;

PARK, DH ;

KIM, K ;

PLAPP, BV ;

KLINMAN, JP .

BIOCHEMISTRY, 1993, 32 (21) :5503-5507

[4] The role of Tyr-169 of trimethylamine dehydrogenase in substrate oxidation and magnetic interaction between FMN cofactor and the 4Fe/4S center [J].

Basran, J ;

Jang, MH ;

Sutcliffe, MJ ;

Hille, R ;

Scrutton, NS .

JOURNAL OF BIOLOGICAL CHEMISTRY, 1999, 274 (19) :13155-13161

[5] Differential coupling through Val-344 and Tyr-442 of trimethylamine dehydrogenase in electron transfer reactions with ferricenium ions and electron transferring flavoprotein [J].

Basran, J ;

Chohan, KK ;

Sutcliffe, MJ ;

Scrutton, NS .

BIOCHEMISTRY, 2000, 39 (31) :9188-9200

[6] Reductive half-reaction of the H172Q mutant of trimethylamine dehydrogenase: evidence against a carbanion mechanism and assignment of kinetically influential ionizations in the enzyme-substrate complex [J].

Basran, J ;

Sutcliffe, MJ ;

Hille, R ;

Scrutton, NS .

BIOCHEMICAL JOURNAL, 1999, 341 :307-314

[7] H-tunneling in the multiple H-transfers of the catalytic cycle of morphinone reductase and in the reductive half-reaction of the homologous pentaerythritol tetranitrate reductase [J].

Basran, J ;

Harris, RJ ;

Sutcliffe, MJ ;

Scrutton, NS .

JOURNAL OF BIOLOGICAL CHEMISTRY, 2003, 278 (45) :43973-43982

[8] Selective modification of alkylammonium ion specificity in trimethylamine dehydrogenase by the rational engineering of cation-pi bonding [J].

Basran, J ;

Mewies, M ;

Mathews, FS ;

Scrutton, NS .

BIOCHEMISTRY, 1997, 36 (08) :1989-1998

[9] Mechanistic aspects of the covalent flavoprotein dimethylglycine oxidase of Arthrobacter globiformis studied by stopped-flow spectrophotometry [J].

Basran, J ;

Bhanji, N ;

Basran, A ;

Nietlispach, D ;

Mistry, S ;

Meskys, R ;

Scrutton, NS .

BIOCHEMISTRY, 2002, 41 (14) :4733-4743

[10] Optimizing the Michaelis complex of trimethylamine dehydrogenase - Identification of interactions that perturb the ionization of substrate and facilitate catalysis with trimethylamine base [J].

Basran, J ;

Sutcliffe, MJ ;

Scrutton, NS .

JOURNAL OF BIOLOGICAL CHEMISTRY, 2001, 276 (46) :42887-42892

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