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Literature summary for 1.3.1.42 extracted from

  • Fox, B.G.; Malone, T.E.; Johnson, K.A.; Madson, S.E.; Aceti, D.; Bingman, C.A.; Blommel, P.G.; Buchan, B.; Burns, B.; Cao, J.; Cornilescu, C.; Doreleijers, J.; Ellefson, J.; Frederick, R.; Geetha, H.; Hruby, D.; Jeon, W.B.; Kimball, T.; Kunert, J.; Markley, J.L.; Newman, C.; Olson, A.; Peterson, F.C.; Phillips, G.N.; Primm, J.; Ramirez, B.; Rosenberg, N.S.; Runnels, M.; Seder, K.; Shaw, J.; Smith, D.W.; Sreenath, H.; Song, J.; Sussman, M.R.; Thao, S.; Troestler, D.; Tyler, E.; Tyler, R.; Ulrich, E.; Vinarov, D.; Vojtik, F.; Volkman, B.F.; Wesenberg, G.; Wrobel, R.L.; Zhang, J.; Zhao, Q.; Zolnai, Z.
    X-ray structure of Arabidopsis At1g77680, 12-oxophytodienoate reductase isoform 1 (2005), Proteins, 61, 206-208.
    View publication on PubMed

Crystallization (Commentary)

Crystallization (Comment) Organism
one enzyme monomer per asymmetric unit, space group C2221. Enzyme is a member of an alpha/beta barrel fold family of FMN-containing oxidoreductases Arabidopsis thaliana

Organism

Organism UniProt Comment Textmining
Arabidopsis thaliana
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isoform OPR1, expression in Escherichia coli
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Cofactor

Cofactor Comment Organism Structure
FMN one molecule per enzyme monomer Arabidopsis thaliana