Kcat Enzymatic Pvt. Ltd.
kcat.co.in
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Ideaspring Capital
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Overview
At Kcat Enzymatic, we constantly work towards ensuring access to high quality and economically viable engineered enzymes to support the reduction in carbon footprint, for sustainability and a greener environment; this is the reason why we have been trusted by leading pharmaceutical companies and enzyme stakeholders across the globe.
News
Multimodal neural network for enhanced protein stability prediction by integration of contact scores and spatial maps
In this study, we developed an AI-driven protein stability prediction framework that integrates AlphaFold-generated structures, molecular refinement, and deep learning techniques. Multiple machine learning and neural network architectures were evaluated,
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Breaking the Scale Barrier in Biocatalyst Development: AI-Powered Enzyme Engineering for Minimal Variants and Commercial Efficiency
In this study, we developed a sustainable biocatalytic process for sitagliptin production using an AI-driven 6D-grid protein engineering platform. By leveraging molecular interaction data, solvent effects, and a database of 1.39 million structural fragmen
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Towards universal synthetic heterotrophy using a metabolic coordinator
Engineering the utilization of non-native substrates, or synthetic heterotrophy, in proven industrial microbes such as Saccharomyces cerevisiae represents an opportunity to valorize plentiful and renewable sources of carbon and energy as inputs to bioproc
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Quantum Molecular Dynamics Study on the Reaction Mechanism of Nitrilase toward an Aliphatic Dinitrile Substrate
This study employed quantum mechanical dynamics (QMD) simulations to elucidate the catalytic mechanism of Bacillus safensis nitrilase (BsNIT) toward pentanedinitrile (PD). The results revealed a sequential conversion of PD to 4-cyanobutanoic acid and subs
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Unraveling the Structure-Function Relationship and Mechanism of an Important Spiro-Forming Nitrilase Using Metadynamics and Quantum Molecular Dynamics
This study provides the first comprehensive computational investigation of the nitrilase from Bacillus safensis (BsNIT) and Spirosoma linguale DSM 74 (SINIT) for elucidation on the reaction mechanism for nitrile hydrolysis and nitrile hydration reaction r
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Reversal of the Leloir pathway to promote galactose and tagatose synthesis from glucose
In this research article, we demonstrate direct conversion of glucose to D-tagatose, a low-calorie rare sugar, using an engineered Escherichia coli whole-cell system. Our study identifies a galactose-1-phosphate phosphatase (DdGal1Pase) with stringent sub
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Computational studies on the catalytic potential of the double active site for enzyme engineering
We're excited to announce our latest publication in Nature Scientific Reports on proteins with double active sites, which could revolutionize enzyme design strategies. We have developed an AI-based tool which creates enzymes with multiple active sites, en
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In Silico Screening of Chlorogenic Acids from Plant Sources against Human Translocase-I to Identify Competitive Inhibitors to Treat Diabetes
Chlorogenic acids (CHLs) are known to competitively bind to translocase-I (T1) of the glucose-6-phosphatase (G6 Pase) system, thereby inhibiting the transport of glucose-6-phosphate (G6P). This competitive binding results in a consequential reduction in b
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In-Depth Sequence-Function Characterization Reveals Multiple Pathways To Enhance Enzymatic Activity
Phenyl Ammonia Lyase (PAL) has garnered significant attention as the active ingredient in Pegvaliase, the only FDA-approved drug for treating classical phenylketonuria (PKU). Highlights: Deep Mutational scanning (DMS) to derive functional hotspots Hybrid
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Structure, dynamics, and molecular inhibition of the Staphylococcus aureus m1A22-tRNA methyltransferase TrmK
The enzyme m1A22-tRNA methyltransferase (TrmK) from Staphylococcus aureus catalyzes the transfer of a methyl group to the N1 of adenine 22 in bacterial tRNAs. TrmK is essential for S. aureus survival during infection, but has no homolog in mammals, making
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Offices
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Bengaluru
India
Engineering / R&D
Biotechnology Lab
Bengaluru, Karnataka 560100.