Any feedback?
Please rate this page
(search_result.php)
(0/150)

BRENDA support

Refine search

Search Reference

show results
Don't show organism specific information (fast!)
Search organism in taxonomic tree (slow, choose "exact" as search mode, e.g. "mammalia" for rat,human,monkey,...)
(Not possible to combine with the first option)
Refine your search
Show additional data
do not include text mining results
include AMENDA results (Automatic Mining of Enzyme Data)
include FRENDA results (AMENDA + additional results, but less precise)

Search term:

Results 1 - 10 of 58 > >>
EC Number BRENDA No. Title Journal Volume Pages Year Organism PubMed ID
Show all pathways known for 2.6.1.52Display the reaction diagram Show all sequences 2.6.1.52758704 Molecular characterization and expression analysis of a phosphoserine aminotransferase involving L-serine synthesis from silkworm, Bombyx mori Arch. Insect Biochem. Physiol. 101 e21553 2019 Bombyx mori 31004387
Show all pathways known for 2.6.1.52Display the reaction diagram Show all sequences 2.6.1.52758704 Molecular characterization and expression analysis of a phosphoserine aminotransferase involving L-serine synthesis from silkworm, Bombyx mori Arch. Insect Biochem. Physiol. 101 e21553 2019 Bombyx mori p50T 31004387
Show all pathways known for 2.6.1.52Display the reaction diagram Show all sequences 2.6.1.52758704 Molecular characterization and expression analysis of a phosphoserine aminotransferase involving L-serine synthesis from silkworm, Bombyx mori Arch. Insect Biochem. Physiol. 101 e21553 2019 Bombyx mori b94 31004387
Show all pathways known for 2.6.1.52Display the reaction diagram Show all sequences 2.6.1.52759344 N-terminal residues are crucial for quaternary structure and active site conformation for the phosphoserine aminotransferase from enteric human parasite E. histolytica Int. J. Biol. Macromol. 132 1012-1023 2019 Entamoeba histolytica 30959130
Show all pathways known for 2.6.1.52Display the reaction diagram Show all sequences 2.6.1.52759344 N-terminal residues are crucial for quaternary structure and active site conformation for the phosphoserine aminotransferase from enteric human parasite E. histolytica Int. J. Biol. Macromol. 132 1012-1023 2019 Entamoeba histolytica HM1:IMSS 30959130
Show all pathways known for 2.6.1.52Display the reaction diagram Show all sequences 2.6.1.52758955 Engineering of phosphoserine aminotransferase increases the conversion of L-homoserine to 4-hydroxy-2-ketobutyrate in a glycerol-independent pathway of 1,3-propanediol production from glucose Biotechnol. J. 14 e1900003 2019 Escherichia coli 30925016
Show all pathways known for 2.6.1.52Display the reaction diagram Show all sequences 2.6.1.52758955 Engineering of phosphoserine aminotransferase increases the conversion of L-homoserine to 4-hydroxy-2-ketobutyrate in a glycerol-independent pathway of 1,3-propanediol production from glucose Biotechnol. J. 14 e1900003 2019 Escherichia coli MG1655 30925016
Show all pathways known for 2.6.1.52Display the reaction diagram Show all sequences 2.6.1.52759886 Comparison of kinetic and enzymatic properties of intracellular phosphoserine aminotransferases from alkaliphilic and neutralophilic bacteria Open Chem. 18 149-164 2020 Bos taurus -
Show all pathways known for 2.6.1.52Display the reaction diagram Show all sequences 2.6.1.52759886 Comparison of kinetic and enzymatic properties of intracellular phosphoserine aminotransferases from alkaliphilic and neutralophilic bacteria Open Chem. 18 149-164 2020 Escherichia coli -
Show all pathways known for 2.6.1.52Display the reaction diagram Show all sequences 2.6.1.52759886 Comparison of kinetic and enzymatic properties of intracellular phosphoserine aminotransferases from alkaliphilic and neutralophilic bacteria Open Chem. 18 149-164 2020 Glycine max -
Results 1 - 10 of 58 > >>