The mechanistic insights into different aspects of promiscuity in metalloenzymes.
Adv Protein Chem Struct Biol
; 141: 23-66, 2024.
Article
in En
| MEDLINE
| ID: mdl-38960476
ABSTRACT
Enzymes are nature's ultimate machinery to catalyze complex reactions. Though enzymes are evolved to catalyze specific reactions, they also show significant promiscuity in reactions and substrate selection. Metalloenzymes contain a metal ion or metal cofactor in their active site, which is crucial in their catalytic activity. Depending on the metal and its coordination environment, the metal ion or cofactor may function as a Lewis acid or base and a redox center and thus can catalyze a plethora of natural reactions. In fact, the versatility in the oxidation state of the metal ions provides metalloenzymes with a high level of catalytic adaptability and promiscuity. In this chapter, we discuss different aspects of promiscuity in metalloenzymes by using several recent experimental and theoretical works as case studies. We start our discussion by introducing the concept of promiscuity and then we delve into the mechanistic insight into promiscuity at the molecular level.
Key words
Full text:
1
Collection:
01-internacional
Database:
MEDLINE
Main subject:
Metalloproteins
Language:
En
Journal:
Adv Protein Chem Struct Biol
Journal subject:
BIOLOGIA
/
BIOQUIMICA
Year:
2024
Document type:
Article
Affiliation country: