Using Steady-State Kinetics to Quantitate Substrate Selectivity and Specificity: A Case Study with Two Human Transaminases
We examined the ability of two human cytosolic transaminases, aspartate aminotransferase (GOT1) and alanine aminotransferase (GPT), to transform their preferred substrates whilst discriminating against similar metabolites. This offers an opportunity to survey our current understanding of enzyme sele...
Main Authors: | Alessio Peracchi, Eugenia Polverini |
---|---|
Format: | Article |
Language: | English |
Published: |
MDPI AG
2022-02-01
|
Series: | Molecules |
Subjects: | |
Online Access: | https://www.mdpi.com/1420-3049/27/4/1398 |
Similar Items
-
A Xylenol Orange-Based Screening Assay for the Substrate Specificity of Flavin-Dependent para-Phenol Oxidases
by: Tom A. Ewing, et al.
Published: (2018-01-01) -
The impact of tunnel mutations on enzymatic catalysis depends on the tunnel-substrate complementarity and the rate-limiting step
by: Piia Kokkonen, et al.
Published: (2020-01-01) -
The Uncommon Active Site of D-Amino Acid Transaminase from <i>Haliscomenobacter hydrossis</i>: Biochemical and Structural Insights into the New Enzyme
by: Alina K. Bakunova, et al.
Published: (2021-08-01) -
Counterbalance of Stability and Activity Observed for Thermostable Transaminase from <i>Thermobaculum terrenum</i> in the Presence of Organic Solvents
by: Ekaterina Yu. Bezsudnova, et al.
Published: (2020-09-01) -
Activity of transaminase enzyme and testosterone hormone in blood of Awassi rams during different season
by: Souhayla Oneeis Hussain, et al.
Published: (2017-01-01)