β-Amyrin synthase from Euphorbia tirucalli. Steric bulk, not the π-electrons of Phe, at position 474 has a key role in affording the correct folding of the substrate to complete the normal polycyclization cascade-Reference-Cited by-同舟云学术

β-Amyrin synthase from Euphorbia tirucalli. Steric bulk, not the π-electrons of Phe, at position 474 has a key role in affording the correct folding of the substrate to complete the normal polycyclization cascade

Published:2014 Issue:23 Volume:12 Page:3836-3846
ISSN:1477-0520
Container-title:Org. Biomol. Chem.
language:en
Short-container-title:Org. Biomol. Chem.

Author:

Ito Ryousuke¹²³⁴⁵,Masukawa Yukari¹²³⁴⁵,Nakada Chika¹²³⁴⁵,Amari Kanako¹²³⁴⁵,Nakano Chiaki¹²³⁴⁵,Hoshino Tsutomu¹²³⁴⁵

Affiliation:

1. Graduate School of Science and Technology

2. and Department of Applied Biological Chemistry

3. Faculty of Agriculture

4. Niigata University

5. Niigata 950-2181, Japan

Abstract

The importance of the steric bulk at 474 residue is described for completion of the cyclization cascade, but not the π-electrons of the Phe residue.

Publisher

Royal Society of Chemistry (RSC)

Subject

Organic Chemistry,Physical and Theoretical Chemistry,Biochemistry

Link

http://pubs.rsc.org/en/content/articlepdf/2014/OB/C4OB00064A

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