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author Rutz, Adriano
Probst, Daniel
Aguilar, César
Akiyama, Daniel Y
Alberti, Fabrizio
Augustijn, Hannah E
Avalon, Nicole E
Beemelmanns, Christine
Barbieri, Hellen Bertoletti
Biermann, Friederike
Bridge, Alan J
Girón, Esteban Charria
Cox, Russell
Crüsemann, Max
D'Agostino, Paul M
Feuermann, Marc
Gerke, Jennifer
García, Karina Gutiérrez
Holme, Jonathan E
Hwang, Ji-Yeon
Iacovelli, Riccardo
Jeronimo Barbosa, Júlio César
Kaur, Navneet
Klapper, Martin
Köhler, Anna M
Korenskaia, Aleksandra
Kubach, Noel
Lee, Byung T
Loureiro, Catarina
Mantri, Shrikant
Narula, Simran
Meijer, David
Navarro-Muñoz, Jorge C
Nguyen, Giang-Son
Paliyal, Sunaina
Panghal, Mohit
Rao, Latika
Sieber, Simon
Sokolova, Nika
Sowa, Sven T
Szenei, Judit
Terlouw, Barbara R
Weddeling, Heiner G
Yu, Jingwei
Ziemert, Nadine
Weber, Tilmann
Blin, Kai
van der Hooft, Justin J J
Medema, Marnix H
Zdouc, Mitja M
author_facet Rutz, Adriano
Probst, Daniel
Aguilar, César
Akiyama, Daniel Y
Alberti, Fabrizio
Augustijn, Hannah E
Avalon, Nicole E
Beemelmanns, Christine
Barbieri, Hellen Bertoletti
Biermann, Friederike
Bridge, Alan J
Girón, Esteban Charria
Cox, Russell
Crüsemann, Max
D'Agostino, Paul M
Feuermann, Marc
Gerke, Jennifer
García, Karina Gutiérrez
Holme, Jonathan E
Hwang, Ji-Yeon
Iacovelli, Riccardo
Jeronimo Barbosa, Júlio César
Kaur, Navneet
Klapper, Martin
Köhler, Anna M
Korenskaia, Aleksandra
Kubach, Noel
Lee, Byung T
Loureiro, Catarina
Mantri, Shrikant
Narula, Simran
Meijer, David
Navarro-Muñoz, Jorge C
Nguyen, Giang-Son
Paliyal, Sunaina
Panghal, Mohit
Rao, Latika
Sieber, Simon
Sokolova, Nika
Sowa, Sven T
Szenei, Judit
Terlouw, Barbara R
Weddeling, Heiner G
Yu, Jingwei
Ziemert, Nadine
Weber, Tilmann
Blin, Kai
van der Hooft, Justin J J
Medema, Marnix H
Zdouc, Mitja M
Rutz, Adriano
Probst, Daniel
Aguilar, César
Akiyama, Daniel Y
Alberti, Fabrizio
Augustijn, Hannah E
Avalon, Nicole E
Beemelmanns, Christine
Barbieri, Hellen Bertoletti
Biermann, Friederike
Bridge, Alan J
Girón, Esteban Charria
Cox, Russell
Crüsemann, Max
D'Agostino, Paul M
Feuermann, Marc
Gerke, Jennifer
García, Karina Gutiérrez
Holme, Jonathan E
Hwang, Ji-Yeon
Iacovelli, Riccardo
Jeronimo Barbosa, Júlio César
Kaur, Navneet
Klapper, Martin
Köhler, Anna M
Korenskaia, Aleksandra
Kubach, Noel
Lee, Byung T
Loureiro, Catarina
Mantri, Shrikant
Narula, Simran
Meijer, David
Navarro-Muñoz, Jorge C
Nguyen, Giang-Son
Paliyal, Sunaina
Panghal, Mohit
Rao, Latika
Sieber, Simon
Sokolova, Nika
Sowa, Sven T
Szenei, Judit
Terlouw, Barbara R
Weddeling, Heiner G
Yu, Jingwei
Ziemert, Nadine
Weber, Tilmann
Blin, Kai
van der Hooft, Justin J J
Medema, Marnix H
Zdouc, Mitja M
collection PubMed - marine biology
contents MITE: the Minimum Information about a Tailoring Enzyme database for capturing specialized metabolite biosynthesis. Rutz, Adriano Probst, Daniel Aguilar, César Akiyama, Daniel Y Alberti, Fabrizio Augustijn, Hannah E Avalon, Nicole E Beemelmanns, Christine Barbieri, Hellen Bertoletti Biermann, Friederike Bridge, Alan J Girón, Esteban Charria Cox, Russell Crüsemann, Max D'Agostino, Paul M Feuermann, Marc Gerke, Jennifer García, Karina Gutiérrez Holme, Jonathan E Hwang, Ji-Yeon Iacovelli, Riccardo Jeronimo Barbosa, Júlio César Kaur, Navneet Klapper, Martin Köhler, Anna M Korenskaia, Aleksandra Kubach, Noel Lee, Byung T Loureiro, Catarina Mantri, Shrikant Narula, Simran Meijer, David Navarro-Muñoz, Jorge C Nguyen, Giang-Son Paliyal, Sunaina Panghal, Mohit Rao, Latika Sieber, Simon Sokolova, Nika Sowa, Sven T Szenei, Judit Terlouw, Barbara R Weddeling, Heiner G Yu, Jingwei Ziemert, Nadine Weber, Tilmann Blin, Kai van der Hooft, Justin J J Medema, Marnix H Zdouc, Mitja M Enzymes Substrate Specificity Software Humans Machine Learning Computational Biology Internet Databases, Protein Secondary or specialized metabolites show extraordinary structural diversity and potent biological activities relevant for clinical and industrial applications. The biosynthesis of these metabolites usually starts with the assembly of a core 'scaffold', which is subsequently modified by tailoring enzymes to define the molecule's final structure and, in turn, its biological activity profile. Knowledge about reaction and substrate specificity of tailoring enzymes is essential for understanding and computationally predicting metabolite biosynthesis, but this information is usually scattered in the literature. Here, we present MITE, the Minimum Information about a Tailoring Enzyme database. MITE employs a comprehensive set of parameters to annotate tailoring enzymes, defining substrate and reaction specificity by the expressive reaction SMARTS (Simplified Molecular Input Line Entry System Arbitrary Target Specification) chemical pattern language. Both human and machine readable, MITE can be used as a knowledge base, for in silico biosynthesis, or to train machine-learning applications, and tightly integrates with existing resources. Designed as a community-driven and open resource, MITE employs a rolling release model of data curation and expert review. MITE is freely accessible at https://mite.bioinformatics.nl/.
format Artículo científico
id pubmed_41001881
institution PubMed
language en
publishDate 2026
publisher Nucleic acids research
record_format pubmed
spellingShingle MITE: the Minimum Information about a Tailoring Enzyme database for capturing specialized metabolite biosynthesis.
Rutz, Adriano
Probst, Daniel
Aguilar, César
Akiyama, Daniel Y
Alberti, Fabrizio
Augustijn, Hannah E
Avalon, Nicole E
Beemelmanns, Christine
Barbieri, Hellen Bertoletti
Biermann, Friederike
Bridge, Alan J
Girón, Esteban Charria
Cox, Russell
Crüsemann, Max
D'Agostino, Paul M
Feuermann, Marc
Gerke, Jennifer
García, Karina Gutiérrez
Holme, Jonathan E
Hwang, Ji-Yeon
Iacovelli, Riccardo
Jeronimo Barbosa, Júlio César
Kaur, Navneet
Klapper, Martin
Köhler, Anna M
Korenskaia, Aleksandra
Kubach, Noel
Lee, Byung T
Loureiro, Catarina
Mantri, Shrikant
Narula, Simran
Meijer, David
Navarro-Muñoz, Jorge C
Nguyen, Giang-Son
Paliyal, Sunaina
Panghal, Mohit
Rao, Latika
Sieber, Simon
Sokolova, Nika
Sowa, Sven T
Szenei, Judit
Terlouw, Barbara R
Weddeling, Heiner G
Yu, Jingwei
Ziemert, Nadine
Weber, Tilmann
Blin, Kai
van der Hooft, Justin J J
Medema, Marnix H
Zdouc, Mitja M
Enzymes
Substrate Specificity
Software
Humans
Machine Learning
Computational Biology
Internet
Databases, Protein
MITE: the Minimum Information about a Tailoring Enzyme database for capturing specialized metabolite biosynthesis. Rutz, Adriano Probst, Daniel Aguilar, César Akiyama, Daniel Y Alberti, Fabrizio Augustijn, Hannah E Avalon, Nicole E Beemelmanns, Christine Barbieri, Hellen Bertoletti Biermann, Friederike Bridge, Alan J Girón, Esteban Charria Cox, Russell Crüsemann, Max D'Agostino, Paul M Feuermann, Marc Gerke, Jennifer García, Karina Gutiérrez Holme, Jonathan E Hwang, Ji-Yeon Iacovelli, Riccardo Jeronimo Barbosa, Júlio César Kaur, Navneet Klapper, Martin Köhler, Anna M Korenskaia, Aleksandra Kubach, Noel Lee, Byung T Loureiro, Catarina Mantri, Shrikant Narula, Simran Meijer, David Navarro-Muñoz, Jorge C Nguyen, Giang-Son Paliyal, Sunaina Panghal, Mohit Rao, Latika Sieber, Simon Sokolova, Nika Sowa, Sven T Szenei, Judit Terlouw, Barbara R Weddeling, Heiner G Yu, Jingwei Ziemert, Nadine Weber, Tilmann Blin, Kai van der Hooft, Justin J J Medema, Marnix H Zdouc, Mitja M Enzymes Substrate Specificity Software Humans Machine Learning Computational Biology Internet Databases, Protein Secondary or specialized metabolites show extraordinary structural diversity and potent biological activities relevant for clinical and industrial applications. The biosynthesis of these metabolites usually starts with the assembly of a core 'scaffold', which is subsequently modified by tailoring enzymes to define the molecule's final structure and, in turn, its biological activity profile. Knowledge about reaction and substrate specificity of tailoring enzymes is essential for understanding and computationally predicting metabolite biosynthesis, but this information is usually scattered in the literature. Here, we present MITE, the Minimum Information about a Tailoring Enzyme database. MITE employs a comprehensive set of parameters to annotate tailoring enzymes, defining substrate and reaction specificity by the expressive reaction SMARTS (Simplified Molecular Input Line Entry System Arbitrary Target Specification) chemical pattern language. Both human and machine readable, MITE can be used as a knowledge base, for in silico biosynthesis, or to train machine-learning applications, and tightly integrates with existing resources. Designed as a community-driven and open resource, MITE employs a rolling release model of data curation and expert review. MITE is freely accessible at https://mite.bioinformatics.nl/.
title MITE: the Minimum Information about a Tailoring Enzyme database for capturing specialized metabolite biosynthesis.
topic Enzymes
Substrate Specificity
Software
Humans
Machine Learning
Computational Biology
Internet
Databases, Protein
url https://pubmed.ncbi.nlm.nih.gov/41001881/