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<< < Results 11 - 20 of 81 > >>
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EC Number Substrates Commentary Substrates Organism Products Commentary (Products) Reversibility
Show all pathways known for 1.17.1.8Display the word mapDisplay the reaction diagram Show all sequences 1.17.1.8(2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + NAD(P)H + H+ the enzyme is involved in L-lysine biosynthesis Corynebacterium glutamicum (S)-2,3,4,5-tetrahydropyridine-2,6-dicarboxylate + NAD(P)+ + H2O - ?
Show all pathways known for 1.17.1.8Display the word mapDisplay the reaction diagram Show all sequences 1.17.1.8(2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + NAD(P)H + H+ it is proposed that the the domain movement for active site constitution occurs when both cofactor and substrate bind to the enzyme Corynebacterium glutamicum (S)-2,3,4,5-tetrahydropyridine-2,6-dicarboxylate + NAD(P)+ + H2O - ?
Show all pathways known for 1.17.1.8Display the word mapDisplay the reaction diagram Show all sequences 1.17.1.8(S)-2,3,4,5-tetrahydropyridine-2,6-dicarboxylate + NAD(P)+ + H2O involved in L-lysine biosynthesis Corynebacterium glutamicum (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + NAD(P)H + H+ - ?
Show all pathways known for 1.17.1.8Display the word mapDisplay the reaction diagram Show all sequences 1.17.1.8(S)-2,3,4,5-tetrahydropyridine-2,6-dicarboxylate + NAD+ + H2O the enzyme utilizes both NADH and NADPH as cofactors Corynebacterium glutamicum (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + NADH + H+ - ?
Show all pathways known for 1.17.1.8Display the word mapDisplay the reaction diagram Show all sequences 1.17.1.8(S)-2,3,4,5-tetrahydropyridine-2,6-dicarboxylate + NADP+ + H2O the enzyme utilizes both NADH and NADPH as cofactors Corynebacterium glutamicum (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + NADPH + H+ - ?
Show all pathways known for 1.17.1.8Display the word mapDisplay the reaction diagram Show all sequences 1.17.1.82,3-dihydrodipicolinate + NAD(P)H - Corynebacterium glutamicum 2,3,4,5-tetrahydrodipicolinate + NAD(P)+ - ?
Show all pathways known for 1.17.1.8Display the word mapDisplay the reaction diagram Show all sequences 1.17.1.8(2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + NAD(P)H + H+ the enzyme is involved in L-lysine biosynthesis Corynebacterium glutamicum ATCC 13032 (S)-2,3,4,5-tetrahydropyridine-2,6-dicarboxylate + NAD(P)+ + H2O - ?
Show all pathways known for 1.17.1.8Display the word mapDisplay the reaction diagram Show all sequences 1.17.1.8(2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + NAD(P)H + H+ it is proposed that the the domain movement for active site constitution occurs when both cofactor and substrate bind to the enzyme Corynebacterium glutamicum ATCC 13032 (S)-2,3,4,5-tetrahydropyridine-2,6-dicarboxylate + NAD(P)+ + H2O - ?
Show all pathways known for 1.17.1.8Display the word mapDisplay the reaction diagram Show all sequences 1.17.1.8(S)-2,3,4,5-tetrahydropyridine-2,6-dicarboxylate + NAD(P)+ + H2O involved in L-lysine biosynthesis Corynebacterium glutamicum ATCC 13032 (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + NAD(P)H + H+ - ?
Show all pathways known for 1.17.1.8Display the word mapDisplay the reaction diagram Show all sequences 1.17.1.8(S)-2,3,4,5-tetrahydropyridine-2,6-dicarboxylate + NAD+ + H2O the enzyme utilizes both NADH and NADPH as cofactors Corynebacterium glutamicum ATCC 13032 (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + NADH + H+ - ?
<< < Results 11 - 20 of 81 > >>
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