Evidence map›Paper›PMID 41272324›Full record

ArticleBiotechnology letters2025

Characterization and substrate specificity study of the novel (R)-amine transaminase MagAT.

Xiaole Yang, Xia Tian, Hai Zhu, Weiwei Jia, Jiahuan Li, Ruizhou Tang, Chuanzhi Zhang, Yang Cao, Tingting Li

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Article in Biotechnology letters, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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1 · What the graph read from it

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2 · The registry

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3 · Its place in the literature

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0 citing papers in PubMed.

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4 · The record

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PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

9 authors.

Xiaole Yang *Jiangsu Key Laboratory of Marine Pharmaceutical Compound Screening, Jiangsu Ocean University, Lianyungang, 222005, China.
Xia Tian *Jiangsu Key Laboratory of Marine Pharmaceutical Compound Screening, Jiangsu Ocean University, Lianyungang, 222005, China.
Hai ZhuJiangsu Key Laboratory of Marine Pharmaceutical Compound Screening, Jiangsu Ocean University, Lianyungang, 222005, China.
Weiwei JiaJiangsu Key Laboratory of Marine Pharmaceutical Compound Screening, Jiangsu Ocean University, Lianyungang, 222005, China.
Jiahuan LiJiangsu Key Laboratory of Marine Pharmaceutical Compound Screening, Jiangsu Ocean University, Lianyungang, 222005, China.
Ruizhou TangJiangsu Key Laboratory of Marine Pharmaceutical Compound Screening, Jiangsu Ocean University, Lianyungang, 222005, China.
Chuanzhi ZhangBio-Pharmaceutical Research Institute Lian Yun Gang Chia Tai Tianqing Pharmaceutical Group Co., Ltd, Lianyungang, 222062, Jiangsu, China.
Yang CaoJiangsu Key Laboratory of Marine Pharmaceutical Compound Screening, Jiangsu Ocean University, Lianyungang, 222005, China.
Tingting LiJiangsu Key Laboratory of Marine Pharmaceutical Compound Screening, Jiangsu Ocean University, Lianyungang, 222005, China. litt@jou.edu.cn.ORCID http://orcid.org/0000-0002-6587-8645

Funding

Jiangsu Collaborative Innovation Center of Chinese Medicinal Resources Industrialization JSIMR202021Jiangsu Ocean University for start-up fund KQ19026Lianyungang Science and Technology Bureau CA202404
6 · The paper itself

Abstract

Chiral amines, as essential chiral building blocks in drug synthesis, present a considerable challenge in biomanufacturing due to the requirement for highly efficient stereoselective synthesis. In this study, we successfully cloned and heterologously expressed a novel (R)-amine transaminase, MagAT, from Mycolicibacterium agri. Systematic analysis showed optimal activity at pH 7.0, with the highest reaction rate occurring within 30 min at 50 ℃. However, considering overall thermal stability, 40℃ was selected as the operating temperature for subsequent experiments. Furthermore, the enzyme retained nearly 100% catalytic activity in the presence of 10% methanol, DMSO, and chloroform. Kinetic analysis demonstrated that MagAT possessed high substrate affinity, with Michaelis constants (K

Indexed as

ActinobacteriaAminesBacterial ProteinsTransaminasesCloning, MolecularEnzyme StabilityHydrogen-Ion ConcentrationKineticsMolecular Docking SimulationRecombinant ProteinsSubstrate SpecificityTemperatureAminesBacterial ProteinsRecombinant ProteinsTransaminasesBiocatalysisChiral aminesGreen chemistry(R)-amine transaminase

Identifiers

PMID41272324

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.