Altering Active-Site Loop Dynamics Enhances Standalone Activity of the Tryptophan Synthase Alpha Subunit

Cristina Duran, Thomas Kinateder, Caroline Hiefinger, Reinhard Sterner, Sílvia Osuna · 2024

Read Altering Active-Site Loop Dynamics Enhances Standalone Activity of the Tryptophan Synthase Alpha Subunit by Cristina Duran, Thomas Kinateder, Caroline Hiefinger, Reinhard Sterner, Sílvia Osuna (2024) in the Tower of Babel, a free online library of public-domain works preserved in clean, searchable text. No sign-up. The full text is served as a plain-text file at a predictable URL, where text is present: https://antarctic-labs.com/tower-of-babel/pmc-11574760.txt.

Description

The α-subunit (TrpA) of the allosterically regulated bifunctional tryptophan synthase αββα enzyme catalyzes the retro-aldol cleavage of indole-glycerol phosphate (IGP) to d-glyceraldehyde 3-phosphate (G3P) and indole. The activity of the enzyme is highly dependent on the β-subunit (TrpB), which allosterically regulates and activates TrpA for enhanced function.

Catalog record

CREATORCristina Duran, Thomas Kinateder, Caroline Hiefinger, Reinhard Sterner, Sílvia Osuna
YEAR2024
COLLECTIONPAPERS
FORMATTXT
FILE SIZE43 KB
VERSION1.0
LICENSECC BY 4.0
RIGHTSCC BY
SOURCEEurope PMC

Source: https://europepmc.org/articles/PMC11574760

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