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Results 1 - 10 of 458 > >>
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EC Number BRENDA No. Title Journal Volume Pages Year Organism PubMed ID
Show all pathways known for 1.5.1.3Display the word mapDisplay the reaction diagram Show all sequences 1.5.1.3765687 Acceleration of catalysis in dihydrofolate reductase by transient, site-specific photothermal excitation Proc. Natl. Acad. Sci. USA 118 e2014592118 2021 Escherichia coli 33468677
Show all pathways known for 1.5.1.3Display the word mapDisplay the reaction diagram Show all sequences 1.5.1.3765363 Adaptations for pressure and temperature in dihydrofolate reductases Microorganisms 9 1706 2021 Escherichia coli 34442785
Show all pathways known for 1.5.1.3Display the word mapDisplay the reaction diagram Show all sequences 1.5.1.3765363 Adaptations for pressure and temperature in dihydrofolate reductases Microorganisms 9 1706 2021 Moritella yayanosii 34442785
Show all pathways known for 1.5.1.3Display the word mapDisplay the reaction diagram Show all sequences 1.5.1.3742518 An active second dihydrofolate reductase enzyme is not a feature of rat and mouse, but they do have activity in their mitochondria FEBS Lett. 589 1855-1862 2015 Homo sapiens 25980602
Show all pathways known for 1.5.1.3Display the word mapDisplay the reaction diagram Show all sequences 1.5.1.3742518 An active second dihydrofolate reductase enzyme is not a feature of rat and mouse, but they do have activity in their mitochondria FEBS Lett. 589 1855-1862 2015 Mus musculus 25980602
Show all pathways known for 1.5.1.3Display the word mapDisplay the reaction diagram Show all sequences 1.5.1.3742518 An active second dihydrofolate reductase enzyme is not a feature of rat and mouse, but they do have activity in their mitochondria FEBS Lett. 589 1855-1862 2015 Rattus norvegicus 25980602
Show all pathways known for 1.5.1.3Display the word mapDisplay the reaction diagram Show all sequences 1.5.1.3742057 Biochemical characterization of the bifunctional enzyme dihydrofolate reductase-thymidylate synthase from Leishmania (Viannia) and its evaluation as a drug target Biomedica 33 393-401 2013 Leishmania braziliensis 24652175
Show all pathways known for 1.5.1.3Display the word mapDisplay the reaction diagram Show all sequences 1.5.1.3742057 Biochemical characterization of the bifunctional enzyme dihydrofolate reductase-thymidylate synthase from Leishmania (Viannia) and its evaluation as a drug target Biomedica 33 393-401 2013 Trypanosoma cruzi 24652175
Show all pathways known for 1.5.1.3Display the word mapDisplay the reaction diagram Show all sequences 1.5.1.3742057 Biochemical characterization of the bifunctional enzyme dihydrofolate reductase-thymidylate synthase from Leishmania (Viannia) and its evaluation as a drug target Biomedica 33 393-401 2013 Leishmania panamensis 24652175
Show all pathways known for 1.5.1.3Display the word mapDisplay the reaction diagram Show all sequences 1.5.1.3763790 Capturing the catalytic proton of dihydrofolate reductase Implications for general acid-Base catalysis ACS Catal. 11 5873-5884 2021 Escherichia coli 34055457
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