INTERPRETATION OF NUCLEAR MAGNETIC-RESONANCE SPECTRA FOR LACTOBACILLUS-CASEI DIHYDROFOLATE-REDUCTASE BASED ON THE X-RAY STRUCTURE OF THE ENZYME-METHOTREXATE-NADPH COMPLEX

被引：25

作者：

MATTHEWS, DA

机构：

[1] Department of Chemistry, University of California, San Diego, La Jolla

来源：

BIOCHEMISTRY | 1979年 / 18卷 / 08期

关键词：

D O I：

10.1021/bi00575a035

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 three-dimensional molecular structure of Lactobacillus casei dihydrofolate reductase complexed with NADPH and methotrexate has been used to interpret published magnetic resonance spectra for this enzyme. Proton resonances from histidine residues and 19F resonances from fluorine-labeled fluorotyrosine and fluorotryptophan dihydrofolate reductase have been assigned in several cases to specific amino acids in the primary sequence. Furthermore, the 31P signals from the pyrophosphate moiety of bound NADPH have been assigned and the large upfield shift for l3C-labeled (at the carboxamide carbon) NADP+ upon binding to the reductase has been explained in terms of desolvation effects. © 1979, American Chemical Society. All rights reserved.

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页码：1602 / 1610

页数：9

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