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Results 1 - 6 of 6
EC Number Substrates Commentary Substrates Organism Products Commentary (Products) Reversibility
Show all pathways known for 1.1.1.385Display the reaction diagram Show all sequences 1.1.1.385(1R,2S,5R,6S)-dihydroanticapsin + NAD+ (1R,2S,5R,6S)-dihydroanticapsin i.e. 3-[(1R,2S,5R,6S)-5-hydroxy-7-oxabicyclo[4.1.0]hept-2-yl]-L-alanine. The enzyme is involved in the biosynthesis of the dipeptide antibiotic bacilysin Bacillus subtilis (1R,2S,6R)-anticapsin + NADH + H+ (1R,2S,6R)-anticapsin i.e. 3-[(1R,2S,6R)-5-oxo-7-oxabicyclo[4.1.0]hept-2-yl]-L-alanine ?
Show all pathways known for 1.1.1.385Display the reaction diagram Show all sequences 1.1.1.385(1R,2S,5R,6S)-dihydroanticapsin + NAD+ (1R,2S,5R,6S)-dihydroanticapsin i.e. 3-[(1R,2S,5R,6S)-5-hydroxy-7-oxabicyclo[4.1.0]hept-2-yl]-L-alanine. Exogenous enzyme is added into crude DELTAbacC extracts and dihydroanticapsin transformation is analyzed by LC-MS. Wild-type extract contains a significant amount of bacilysin and a minor amount of anticapsin, but the DELTA extract does not possess a detectable amount of either. However, the DELTAbacC extract contains accumulated amounts of masses corresponding to dihydroanticapsin and dihydrobacilysin, which contain the intact epoxide but possess a C7-hydroxyl moiety in place of the C7-ketone found in mature anticapsin and bacilysin. This finding is consistent with the assignment of the enzyme (BacC) as the dehydrogenase used to oxidize the C7-hydroxyl and strongly suggests that the enzyme (BacC) oxidation occurs sometime after the epoxidation of the cyclohexenol double bond. When the DELTAbacC extract is exposed to the enzyme (BacC) the C7-hydroxyl of hydroanticapsin is oxidized to generate anticapsin. The enzyme (BacC) has no oxidation activity on the dihydrobacilysin dipeptide Bacillus subtilis (1R,2S,6R)-anticapsin + NADH + H+ (1R,2S,6R)-anticapsin i.e. 3-[(1R,2S,6R)-5-oxo-7-oxabicyclo[4.1.0]hept-2-yl]-L-alanine ?
Show all pathways known for 1.1.1.385Display the reaction diagram Show all sequences 1.1.1.385(1R,2S,5R,6S)-dihydroanticapsin + NAD+ (1R,2S,5R,6S)-dihydroanticapsin i.e. 3-[(1R,2S,5R,6S)-5-hydroxy-7-oxabicyclo[4.1.0]hept-2-yl]-L-alanine. The enzyme is involved in the biosynthesis of the dipeptide antibiotic bacilysin Bacillus subtilis 168 (1R,2S,6R)-anticapsin + NADH + H+ (1R,2S,6R)-anticapsin i.e. 3-[(1R,2S,6R)-5-oxo-7-oxabicyclo[4.1.0]hept-2-yl]-L-alanine ?
Show all pathways known for 1.1.1.385Display the reaction diagram Show all sequences 1.1.1.385(1R,2S,5R,6S)-dihydroanticapsin + NAD+ (1R,2S,5R,6S)-dihydroanticapsin i.e. 3-[(1R,2S,5R,6S)-5-hydroxy-7-oxabicyclo[4.1.0]hept-2-yl]-L-alanine. Exogenous enzyme is added into crude DELTAbacC extracts and dihydroanticapsin transformation is analyzed by LC-MS. Wild-type extract contains a significant amount of bacilysin and a minor amount of anticapsin, but the DELTA extract does not possess a detectable amount of either. However, the DELTAbacC extract contains accumulated amounts of masses corresponding to dihydroanticapsin and dihydrobacilysin, which contain the intact epoxide but possess a C7-hydroxyl moiety in place of the C7-ketone found in mature anticapsin and bacilysin. This finding is consistent with the assignment of the enzyme (BacC) as the dehydrogenase used to oxidize the C7-hydroxyl and strongly suggests that the enzyme (BacC) oxidation occurs sometime after the epoxidation of the cyclohexenol double bond. When the DELTAbacC extract is exposed to the enzyme (BacC) the C7-hydroxyl of hydroanticapsin is oxidized to generate anticapsin. The enzyme (BacC) has no oxidation activity on the dihydrobacilysin dipeptide Bacillus subtilis 168 (1R,2S,6R)-anticapsin + NADH + H+ (1R,2S,6R)-anticapsin i.e. 3-[(1R,2S,6R)-5-oxo-7-oxabicyclo[4.1.0]hept-2-yl]-L-alanine ?
Show all pathways known for 1.1.1.385Display the reaction diagram Show all sequences 1.1.1.385(2S,4S,7R)-tetrahydrotyrosine + NAD+ (2S,4S,7R)-tetrahydrotyrosine is a surrogate substrate for the enzyme, because currently there is no route for purifying dihydroanticapsin (with the epoxide intact) from DELTAbacC strain extracts. No activity with (2S,4R,7R)-tetrahydrotyrosine Bacillus subtilis 3-[(1S)-4-oxocyclohex-2-en-1-yl]-L-alanine + NADH + H+ - ?
Show all pathways known for 1.1.1.385Display the reaction diagram Show all sequences 1.1.1.385(2S,4S,7R)-tetrahydrotyrosine + NAD+ (2S,4S,7R)-tetrahydrotyrosine is a surrogate substrate for the enzyme, because currently there is no route for purifying dihydroanticapsin (with the epoxide intact) from DELTAbacC strain extracts. No activity with (2S,4R,7R)-tetrahydrotyrosine Bacillus subtilis 168 3-[(1S)-4-oxocyclohex-2-en-1-yl]-L-alanine + NADH + H+ - ?
Results 1 - 6 of 6