Intersubunit Location of the Active Site of Farnesyl Diphosphate Synthase: Reconstruction of Active Enzymes by Hybrid-Type Heteromeric Dimers of Site-Directed Mutants-Reference-Cited by-同舟云学术

Intersubunit Location of the Active Site of Farnesyl Diphosphate Synthase: Reconstruction of Active Enzymes by Hybrid-Type Heteromeric Dimers of Site-Directed Mutants

Published:1999-12-17 Issue:2 Volume:39 Page:463-469
ISSN:0006-2960
Container-title:Biochemistry
language:en
Short-container-title:Biochemistry

Author:

Koyama Tanetoshi¹,Gotoh Yukio¹,Nishino Tokuzo¹

Affiliation:

1. Institute for Chemical Reaction Science, Tohoku University, Katahira 2-1-1, Aoba-ku, Sendai 980-8577, and Department of Biochemistry and Engineering, Tohoku University, Aramaki Aoba, Aoba-ku, Sendai 980-8579, Japan

Publisher

American Chemical Society (ACS)

Subject

Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/bi991621b

Reference35 articles.

1. Enzymatic Aspects of Isoprenoid Chain Elongation

2. Koyama, T., and Ogura, K. (1999) inComprehensive Natural Products Chemistry(Barton, D., and Nakanishi, K., Eds.) Vol. 2, pp 69−96, Elsevier Science Ltd., Oxford, U.K.

3. Isolation and sequence of the human farnesyl pyrophosphate synthetase cDNA. Coordinate regulation of the mRNAs for farnesyl pyrophosphate synthetase, 3-hydroxy-3-methylglutaryl coenzyme A reductase, and 3-hydroxy-3-methylglutaryl coenzyme A synthase by phorbol ester.

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