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Literature summary for 1.14.13.187 extracted from

  • Li, Y.; Ding, L.; Zhang, Q.; Wang, W.
    MD and QM/MM study on catalytic mechanism of a FAD-dependent enzyme ORF36: For nitro sugar biosynthesis (2013), J. Mol. Graph. Model., 44, 9-16.
    View publication on PubMed

Organism

Organism UniProt Comment Textmining
Micromonospora sp. B5APQ9
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Micromonospora sp. ATCC 39149 B5APQ9
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
TDP-L-epi-vancosamine + 2 NADPH + 2 H+ + 2 O2 enzyme catalyzes a two-step-oxidation. For the second oxidation step, three elementary catalytic steps are found, i.e. a hydroxylation step, a hydrogen back-transfer step and a hydroxyl group elimination step. The hydroxylation step is the rate-determining step with an energy barrier of 26.3 kcal/mol. An oxygen atom from the coenzyme FADHOOH is inserted into the product. Groups Gly132/Ala133/Leu134, Met375/Gln376 and a water fence play a key role in facilitating the rate-determining step. Residues Leu160, Val161 and Ser162 are critical to suppress the rate-determining step Micromonospora sp. ? + 2 NADP+ + 3 H2O
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?
TDP-L-epi-vancosamine + 2 NADPH + 2 H+ + 2 O2 enzyme catalyzes a two-step-oxidation. For the second oxidation step, three elementary catalytic steps are found, i.e. a hydroxylation step, a hydrogen back-transfer step and a hydroxyl group elimination step. The hydroxylation step is the rate-determining step with an energy barrier of 26.3 kcal/mol. An oxygen atom from the coenzyme FADHOOH is inserted into the product. Groups Gly132/Ala133/Leu134, Met375/Gln376 and a water fence play a key role in facilitating the rate-determining step. Residues Leu160, Val161 and Ser162 are critical to suppress the rate-determining step Micromonospora sp. ATCC 39149 ? + 2 NADP+ + 3 H2O
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?

Synonyms

Synonyms Comment Organism
nitrososynthase
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Micromonospora sp.

Cofactor

Cofactor Comment Organism Structure
FAD residues L160 ans F374 are involved in binding Micromonospora sp.