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Literature summary extracted from

  • Snow, A.J.D.; Sharma, M.; Lingford, J.P.; Zhang, Y.; Mui, J.W.; Epa, R.; Goddard-Borger, E.D.; Williams, S.J.; Davies, G.J.
    The sulfoquinovosyl glycerol binding protein SmoF binds and accommodates plant sulfolipids (2022), Curr. Res. Struct. Biol., 4, 51-58 .
    View publication on PubMedView publication on EuropePMC

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.14.14.181 6-sulfo-D-quinovose + FMNH2 + O2 Novosphingobium aromaticivorans
-
 6-dehydro-D-glucose + FMN + sulfite + H2O
-
 ?
1.14.14.181 6-sulfo-D-quinovose + FMNH2 + O2 Novosphingobium aromaticivorans DSM 12444
-
 6-dehydro-D-glucose + FMN + sulfite + H2O
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
1.14.14.181 Novosphingobium aromaticivorans
-
-
-
1.14.14.181 Novosphingobium aromaticivorans DSM 12444
-
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.14.14.181 6-sulfo-D-quinovose + FMNH2 + O2
-
 Novosphingobium aromaticivorans 6-dehydro-D-glucose + FMN + sulfite + H2O
-
 ?
1.14.14.181 6-sulfo-D-quinovose + FMNH2 + O2
-
 Novosphingobium aromaticivorans DSM 12444 6-dehydro-D-glucose + FMN + sulfite + H2O
-
 ?

Synonyms

EC Number Synonyms Comment Organism
1.14.14.181 squD
-
 Novosphingobium aromaticivorans

Cofactor

EC Number Cofactor Comment Organism Structure
1.14.14.181 FMN
-
 Novosphingobium aromaticivorans
1.14.14.181 FMNH2
-
 Novosphingobium aromaticivorans

General Information

EC Number General Information Comment Organism
1.14.14.181 physiological function in Novosphingobium aromaticivorans, sulfoquinovose degradation involves oxygenolytic C-S cleavage by flavin-dependent alkanesulfonate monooxygenase SquD that catalyzes sulfoquinovose cleavage into sulfite and 6-dehydro-D-glucose. SquF is an NAD(P)-dependent D-glucose 6-dehydrogenase Novosphingobium aromaticivorans