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Results 1 - 10 of 14 > >>
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EC Number Substrates Commentary Substrates Organism Products Commentary (Products) Reversibility
Show all pathways known for 6.3.3.6Display the word mapDisplay the reaction diagram Show all sequences 6.3.3.6ATP + (2R,5R)-5-carboxymethylproline low activity, kcat/Km is 2% compared to the value for (2S,5S)-5-carboxymethylproline Pectobacterium carotovorum ? - ?
Show all pathways known for 6.3.3.6Display the word mapDisplay the reaction diagram Show all sequences 6.3.3.6ATP + (2S,5R)-5-carboxymethylproline low activity, kcat/Km is 2% compared to the value for (2S,5S)-5-carboxymethylproline Pectobacterium carotovorum ? - ?
Show all pathways known for 6.3.3.6Display the word mapDisplay the reaction diagram Show all sequences 6.3.3.6ATP + (2S,5S)-5-carboxymethylproline - Pectobacterium carotovorum AMP + diphosphate + (3S,5S)-carbapenam 3-carboxylate - ?
Show all pathways known for 6.3.3.6Display the word mapDisplay the reaction diagram Show all sequences 6.3.3.6ATP + (2S,5S)-5-carboxymethylproline - Streptomyces cattleya AMP + diphosphate + (3S,5S)-carbapenam 3-carboxylate - ?
Show all pathways known for 6.3.3.6Display the word mapDisplay the reaction diagram Show all sequences 6.3.3.6ATP + (2S,5S)-5-carboxymethylproline the enzyme catalyzes the formation of the beta-lactam ring in (5R)-carbapenem-3-carboxylic acid biosynthesis Pectobacterium carotovorum AMP + diphosphate + (3S,5S)-carbapenam 3-carboxylate - ?
Show all pathways known for 6.3.3.6Display the word mapDisplay the reaction diagram Show all sequences 6.3.3.6ATP + (2S,5S)-5-carboxymethylproline the enzyme is involved in the biosynthesis of the carbapenem beta-lactam antibiotic (5R)-carbapen-2-em-3-carboxylate Pectobacterium carotovorum AMP + diphosphate + (3S,5S)-carbapenam 3-carboxylate - ?
Show all pathways known for 6.3.3.6Display the word mapDisplay the reaction diagram Show all sequences 6.3.3.6ATP + (2S,5S)-5-carboxymethylproline a mechanism is proposed where the rate-limiting step is beta-lactam ring formation coupled to a protein conformational change. The role of K443 throughout the reaction is undercored Pectobacterium carotovorum AMP + diphosphate + (3S,5S)-carbapenam 3-carboxylate - ?
Show all pathways known for 6.3.3.6Display the word mapDisplay the reaction diagram Show all sequences 6.3.3.6ATP + (2S,5S)-5-carboxymethylproline catalytic Tyr-Glu dyad is demonstrated by site-directed mutagenesis and kinetic experiments that compare the wild-type enzymes to their respective mutant proteins using pHย–rate profiles, 32P-incorporation experiments, solvent isotope effects, proton inventory, and viscosity variation Pectobacterium carotovorum AMP + diphosphate + (3S,5S)-carbapenam 3-carboxylate - ?
Show all pathways known for 6.3.3.6Display the word mapDisplay the reaction diagram Show all sequences 6.3.3.6ATP + (2S,5S)-5-carboxymethylproline the kinetic mechanism is bi-ter where ATP is the first substrate to bind followed by (2S,5S)-5-carboxymethyl proline and diphosphate is the last product released. Low activity with (2S,5R)-5-carboxymethylproline or (2R,5R)-5-carboxymethylproline Pectobacterium carotovorum AMP + diphosphate + (3S,5S)-carbapenam 3-carboxylate - ?
Show all pathways known for 6.3.3.6Display the word mapDisplay the reaction diagram Show all sequences 6.3.3.6ATP + (2S,6R)-2,6-dimethyl-t-carboxymethylproline - Pectobacterium carotovorum AMP + diphosphate + (3S,5S,6R)-3,6-dimethylcabapenam-3-carboxylate - ?
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