- BRENDA Enzyme Database
The JSON download file for Release 2024 1 is now online, featuring an optimized and updated format The download is available here: https: www brenda-enzymes org download php Please refer to the JSON schema documentation for details on the format change
- Pathway maps - BRENDA Enzyme Database
You can search for pathways, metabolites, enzymes, or BRENDA IDs in the Search Highlight section by start typing your search term Metabolite or reaction search starts when at least 3 characters are entered and support both, the shown label or common name (from tooltip)
- Advanced Search - BRENDA Enzyme Database
BRENDA support Advanced Search Organism: (synonyms, domain, kingdom, phylum, class or order) (e g eukarya, animals, chordata or primates) Search for sepecific enzyme or organism EC Number: use * as a wildcard Enzyme Name: Search in text fields 4 is the maximum of searchable text fields!
- All enzymes - BRENDA Enzyme Database
All enzymes in BRENDA For a more structured view of enzymes EC Numbers and enhanced search capabilities please go to the EC Explorer Number of different enzymes: 8697
- BRENDA download - BRENDA Enzyme Database
Download BRENDA All copyrightable parts of BRENDA are licensed under Creative Commons Attribution License 4 0 (CC BY 4 0) Before downloading any files from BRENDA, you have to actively accept the license
- Enzyme Database - BRENDA
BRENDA - The Comprehensive Enzyme Information System Use of this online version of BRENDA is free under the CC BY 4 0 license
- Login - BRENDA Enzyme Database
Use of this online version of BRENDA is free under the CC BY 4 0 license See terms of use for full details
- Information on EC 1. 1. 1. 27 - L-lactate dehydrogenase - BRENDA Enzyme . . .
BRENDA - The Comprehensive Enzyme Information System the enzyme-NADH-pyruvate ternery complex undergoes a rate-limiting conformational change, in which the substrate loop closes to form a desolvated ternary complex in order to bring the catalytic residue Arg109 into the active site, the catalytic residues Arg109, Asp168, and His195 are highly conserved, catalyic mechanism, detailed overview
|