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<< < Results 11 - 16 of 16
EC Number Natural Substrates Commentary (Nat. Sub.)
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 essentially involved in cell wall synthesis
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 repressed by lysine
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 second step in the biosynthesis of meso-diaminopimelate, a bacterial cell wall component, and is involved in L-lysine biosynthesis
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 enzyme is a part of the biosynthetic pathway leading to meso-diaminopimelic acid and L-lysine in bacteria and higher plants
Show all pathways known for 1.17.1.8Display the word mapDisplay the reaction diagram Show all sequences 1.17.1.8dihydrodipicolinate + NADH + H+ substrate dihydrodipicolinate is instable
Show all pathways known for 1.17.1.8Display the word mapDisplay the reaction diagram Show all sequences 1.17.1.8more DHDPR accepts (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid as true substrate rather than dihydrodipicolinate, suggesting that DHDPR catalyzes an overall deoxygenation reaction, likely by a dehydratase-reductase route, substrate specificity, overview. A critical role is played by residue His 159 in the catalytic mechanism of DHDPR. Replacement of this residue with an alanine or a glutamine is reported to result in a 150-200fold reduction in catalytic rate as well as a 6fold increase in KM. His 159 has been proposed to act as a general acid during catalysis, providing the proton required after hydride addition. No activity with beta-hydroxypyruvate and 3-fluoropyruvate
<< < Results 11 - 16 of 16