A single site mutation can induce functional promiscuity in homoserine kinase-Reference-Cited by-同舟云学术

A single site mutation can induce functional promiscuity in homoserine kinase

Published:2023 Issue:22 Volume:21 Page:4648-4655
ISSN:1477-0520
Container-title:Organic & Biomolecular Chemistry
language:en
Short-container-title:Org. Biomol. Chem.

Author:

Tripathi Ankita¹^ORCID,Dubey Kshatresh Dutta¹^ORCID

Affiliation:

1. Department of Chemistry, School of Natural Sciences, Shiv Nadar Institution of Eminence, Gautam Buddha Nagar, Uttar Pradesh, 201314, India

Abstract

l-Homoserine kinase is crucial in the biosynthesis of l-threonine, l-isoleucine, and l-methionine, where it catalyzes ATP-dependent phosphorylation of l-homoserine (Hse) to yield l-homoserine phosphate as its native activity.

Funder

Department of Biotechnology, Ministry of Science and Technology, India

Publisher

Royal Society of Chemistry (RSC)

Subject

Organic Chemistry,Physical and Theoretical Chemistry,Biochemistry

Link

http://pubs.rsc.org/en/content/articlepdf/2023/OB/D3OB00459G

Reference44 articles.

1. An evolutionary biochemist's perspective on promiscuity

2. Enzyme Promiscuity: A Mechanistic and Evolutionary Perspective

3. Enzyme promiscuity: mechanism and applications

4. The importance of catalytic promiscuity for enzyme design and evolution

5. Structure and Cooperativity in Substrate–Enzyme Interactions: Perspectives on Enzyme Engineering and Inhibitor Design

Cited by 1 articles. 订阅此论文施引文献订阅此论文施引文献，注册后可以免费订阅5篇论文的施引文献，订阅后可以查看论文全部施引文献

1. The mechanistic insights into different aspects of promiscuity in metalloenzymes;Advances in Protein Chemistry and Structural Biology;2024