Highly efficient biosynthesis of isonicotinamide through a substrate access tunnel engineered nitrile hydratase from <i>Carbonactinospora thermoautotrophicus</i>

Guo, Junling; Cheng, Zhongyi; Pepłowski, Łukasz; Zhou, Zhemin

doi:10.1039/d3nj00331k

New J. Chem.

2023

DOI: 10.1039/d3nj00331k

|View full text |Cite

Highly efficient biosynthesis of isonicotinamide through a substrate access tunnel engineered nitrile hydratase from Carbonactinospora thermoautotrophicus

Junling Guo¹,

Zhongyi Cheng²,

Łukasz Pepłowski³

et al.

Abstract: Isonicotinamide has important roles and application prospects in pharmaceutical, medical, and material sciences. The biosynthesis of isonicotinamide has great advantages over chemical methods, but the biosynthesis of isonicotinamide has been...

Help me understand this report

Search citation statements

Order By: Relevance

Paper Sections

Select...

Citation Types

Supporting

Mentioning

Contrasting

Year Published

2024

Publication Types

Select...

Article1

Relationship

Self Cite0

Independent1

Authors

Journals

Cited by 1 publication

References 31 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

Multi-method analysis revealed the mechanism of substrate selectivity in NHase: A gatekeeper residue at the activity center

Meng,

Peplowski,

et al. 2024

International Journal of Biological Macromolecules

View full text Add to dashboard Cite

Multi-method analysis revealed the mechanism of substrate selectivity in NHase: A gatekeeper residue at the activity center

Meng,

Peplowski,

et al. 2024

International Journal of Biological Macromolecules

View full text Add to dashboard Cite

scite is a Brooklyn-based organization that helps researchers better discover and understand research articles through Smart Citations–citations that display the context of the citation and describe whether the article provides supporting or contrasting evidence. scite is used by students and researchers from around the world and is funded in part by the National Science Foundation and the National Institute on Drug Abuse of the National Institutes of Health.

Contact Info

customersupport@researchsolutions.com

10624 S. Eastern Ave., Ste. A-614

Henderson, NV 89052, USA

This site is protected by reCAPTCHA and the Google Privacy Policy and Terms of Service apply.

Blog Terms and Conditions API Terms Privacy Policy Contact Cookie Preferences Do Not Sell or Share My Personal Information

Made with 💙 for researchers

Part of the Research Solutions Family.

Highly efficient biosynthesis of isonicotinamide through a substrate access tunnel engineered nitrile hydratase from Carbonactinospora thermoautotrophicus

Abstract: Isonicotinamide has important roles and application prospects in pharmaceutical, medical, and material sciences. The biosynthesis of isonicotinamide has great advantages over chemical methods, but the biosynthesis of isonicotinamide has been...

Cited by 1 publication

References 31 publications

Multi-method analysis revealed the mechanism of substrate selectivity in NHase: A gatekeeper residue at the activity center

Multi-method analysis revealed the mechanism of substrate selectivity in NHase: A gatekeeper residue at the activity center

Contact Info

Product

Resources

About