AI-DeZyme™ Protein Design Tool

Overview

The AI-DeZyme™ protein design tool is an online software enabling site-directed, random, and combinatorial mutagenesis in a sustainable way. This AI-driven online design tool, developed by GenScript’s bioinformatics team, is based on an exclusively patented algorithm for protein mutagenesis and integrated with our extensive enzyme parameter predictions database.

With up-to-date, state-of-the-art technology, this automated and intelligent application platform helps you rapidly understand, design, and lock in the most ideal variants faster based on the original protein sequence and property strategy you choose. Once desirable candidates are selected by properties score ranking, users have access to create a quote directly for high throughput protein production and verification. Overall, for customers anticipating expressing and screening a large number of candidates, this tool can decrease R&D efforts, time, and cost and simultaneously enhance predictability and efficiency. Therefore, we facilitate the whole process from enzyme prediction to enzyme discovery and enzyme screening.

Highlights

Accelerate Your Project

Complete one round of optimization as fast as 1 hour!

Minimize the Experimental Burden

Design high performance mutants with excellent design accuracy!

One-stop Enzyme Engineering Solution

Cover the entire engineering process from design to production!

Remove the Pressure of IT Infrastructure

Run the algorithm with our GPU!

Patented Algorithm Driven Design

Optimize multiple properties simultaneously!

Case Studies

• Case 1: T7 RNA polymerase_ Patented project

  Definition

  T7 RNA polymerase (E.C.2.7.7.6) is a monomeric phage-produced RNA polymerase widely used to express heterologous genes under the control of the T7 promoter for in vivo and in vitro experiments.

  Application

  Gene and cell therapy, genome engineering, enzyme replacement therapy, and mRNA vaccine development.

  

  Engineering purpose

  Protein engineering aims to find T7 RNA polymerase mutants that can efficiently incorporate modified nucleotides and increase TN polymerase activity, achieve the purpose of large-scale transcription of modified RNA in vitro.

  AI-DeZyme™ design

  With AI-DeZyme™ platform, more than 103 T7 RNA polymerase mutants were obtained. Targeted candidates were screened based on AI evaluation, enzyme expression and related properties were tested.

  Verification Results

  • In this customized, optimized project, we generated 10 candidates and tested 3 among them. The engineered T7 RNA polymerase variants showed higher performance:
    • IVT yield improve 12%
    • mRNA integrity improve 17%
    • mRNA PolyA integrity improve 1.8%
    • dsRNA residue decrease 73%

  • mRNA quality detection:

    

    

    

    
• Case 2: Protease_Standard project

  We optimized protease according to benchmark sequence and took stability as the main optimization index. After obtaining multiple protease mutants through the AI-DeZyme™ platform, we selected 14 candidates for enzyme property testing and the results are shown in the bar table.

  

  Optimization results：

  • The success rate of stability optimization is 64.3%.
  • Candidate P9’s activity and stability were enhanced
• Case 3: Amylase_Standard project

  We optimized amylase according to benchmark sequence and took stability as the main optimization index while maintaining activity. After obtaining multiple amylase mutants through the AI-DeZyme™ platform, we selected 20 candidates for enzyme property testing and the results are shown in the bar table.

  

  Optimization results：

  • The success rate of stability optimization is 30.0%.
  • 20% of the candidates had improved stability and activity.
  • Candidate P9’s activity and stability were enhanced.

Customer Testimonial

"Based on our whole-cell biotransformation results, all mutants show good activity. For compounds that were converted well by the wild-type, mutant 1 had ~1.4-fold increase against two of these compounds. Mutant 1 had ~1.4-3.5-fold higher activity compared to the wild-type, against a few compounds within this panel, and also demonstrates new activity not seen in the wild-type. "

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Fermentation Scientist

from a Biotechnology Company in UK