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Results 1 - 10 of 95 > >>
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EC Number BRENDA No. Title Journal Volume Pages Year Organism PubMed ID
Show all pathways known for 4.1.1.11Display the word mapDisplay the reaction diagram Show all sequences 4.1.1.11749304 Aspartate decarboxylase is required for a normal pupa pigmentation pattern in the silkworm, Bombyx mori Sci. Rep. 5 10885 2015 Bombyx mori 26077025
Show all pathways known for 4.1.1.11Display the word mapDisplay the reaction diagram Show all sequences 4.1.1.11749207 Glu56Ser mutation improves the enzymatic activity and catalytic stability of Bacillus subtilis L-aspartate alpha-decarboxylase for an efficient beta-alanine production Process Biochem. 70 117-123 2018 Escherichia coli -
Show all pathways known for 4.1.1.11Display the word mapDisplay the reaction diagram Show all sequences 4.1.1.11749207 Glu56Ser mutation improves the enzymatic activity and catalytic stability of Bacillus subtilis L-aspartate alpha-decarboxylase for an efficient beta-alanine production Process Biochem. 70 117-123 2018 Bacillus subtilis -
Show all pathways known for 4.1.1.11Display the word mapDisplay the reaction diagram Show all sequences 4.1.1.11749207 Glu56Ser mutation improves the enzymatic activity and catalytic stability of Bacillus subtilis L-aspartate alpha-decarboxylase for an efficient beta-alanine production Process Biochem. 70 117-123 2018 Lactiplantibacillus plantarum -
Show all pathways known for 4.1.1.11Display the word mapDisplay the reaction diagram Show all sequences 4.1.1.11749207 Glu56Ser mutation improves the enzymatic activity and catalytic stability of Bacillus subtilis L-aspartate alpha-decarboxylase for an efficient beta-alanine production Process Biochem. 70 117-123 2018 Corynebacterium glutamicum -
Show all pathways known for 4.1.1.11Display the word mapDisplay the reaction diagram Show all sequences 4.1.1.11749207 Glu56Ser mutation improves the enzymatic activity and catalytic stability of Bacillus subtilis L-aspartate alpha-decarboxylase for an efficient beta-alanine production Process Biochem. 70 117-123 2018 Bacillus subtilis 168 -
Show all pathways known for 4.1.1.11Display the word mapDisplay the reaction diagram Show all sequences 4.1.1.11749207 Glu56Ser mutation improves the enzymatic activity and catalytic stability of Bacillus subtilis L-aspartate alpha-decarboxylase for an efficient beta-alanine production Process Biochem. 70 117-123 2018 Corynebacterium glutamicum ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025 -
Show all pathways known for 4.1.1.11Display the word mapDisplay the reaction diagram Show all sequences 4.1.1.11749207 Glu56Ser mutation improves the enzymatic activity and catalytic stability of Bacillus subtilis L-aspartate alpha-decarboxylase for an efficient beta-alanine production Process Biochem. 70 117-123 2018 Lactiplantibacillus plantarum ATCC BAA-793 / NCIMB 8826 / WCFS1 -
Show all pathways known for 4.1.1.11Display the word mapDisplay the reaction diagram Show all sequences 4.1.1.11747593 Characterization of L-aspartate-alpha-decarboxylase from Bacillus subtilis Chin. J. Biotechnol. 31 1184-1193 2015 Escherichia coli 26762040
Show all pathways known for 4.1.1.11Display the word mapDisplay the reaction diagram Show all sequences 4.1.1.11747593 Characterization of L-aspartate-alpha-decarboxylase from Bacillus subtilis Chin. J. Biotechnol. 31 1184-1193 2015 Bacillus subtilis 26762040
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