The Enzyme Database

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EC 1.7.3.2     
Accepted name: acetylindoxyl oxidase
Reaction: N-acetylindoxyl + O2 = N-acetylisatin + (?)
Systematic name: N-acetylindoxyl:oxygen oxidoreductase
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 9029-37-2
References:
1.  Beevers, H. and French, R.C. Oxidation of N-acetylindoxyl by an enzyme from plants. Arch. Biochem. Biophys. 50 (1954) 427–439. [DOI] [PMID: 13159343]
[EC 1.7.3.2 created 1961]
 
 
EC 2.1.1.212     
Accepted name: 2,7,4′-trihydroxyisoflavanone 4′-O-methyltransferase
Reaction: S-adenosyl-L-methionine + 2,4′,7-trihydroxyisoflavanone = S-adenosyl-L-homocysteine + 2,7-dihydroxy-4′-methoxyisoflavanone
For diagram of daidzein biosynthesis, click here
Other name(s): SAM:2,7,4′-trihydroxyisoflavanone 4′-O-methyltransferase; HI4′OMT; HMM1; MtIOMT5; S-adenosyl-L-methionine:2,7,4′-trihydroxyisoflavanone 4′-O-methyltransferase
Systematic name: S-adenosyl-L-methionine:2,4′,7-trihydroxyisoflavanone 4′-O-methyltransferase
Comments: Specifically methylates 2,4′,7-trihydroxyisoflavanone on the 4′-position. No activity with isoflavones [2]. The enzyme is involved in formononetin biosynthesis in legumes [1]. The protein from pea (Pisum sativum) also methylates (+)-6a-hydroxymaackiain at the 3-position (cf. EC 2.1.1.270, (+)-6a-hydroxymaackiain 3-O-methyltransferase) [4].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Akashi, T., Sawada, Y., Shimada, N., Sakurai, N., Aoki, T. and Ayabe, S. cDNA cloning and biochemical characterization of S-adenosyl-L-methionine: 2,7,4′-trihydroxyisoflavanone 4′-O-methyltransferase, a critical enzyme of the legume isoflavonoid phytoalexin pathway. Plant Cell Physiol. 44 (2003) 103–112. [PMID: 12610212]
2.  Deavours, B.E., Liu, C.J., Naoumkina, M.A., Tang, Y., Farag, M.A., Sumner, L.W., Noel, J.P. and Dixon, R.A. Functional analysis of members of the isoflavone and isoflavanone O-methyltransferase enzyme families from the model legume Medicago truncatula. Plant Mol. Biol. 62 (2006) 715–733. [DOI] [PMID: 17001495]
3.  Liu, C.J., Deavours, B.E., Richard, S.B., Ferrer, J.L., Blount, J.W., Huhman, D., Dixon, R.A. and Noel, J.P. Structural basis for dual functionality of isoflavonoid O-methyltransferases in the evolution of plant defense responses. Plant Cell 18 (2006) 3656–3669. [DOI] [PMID: 17172354]
4.  Akashi, T., VanEtten, H.D., Sawada, Y., Wasmann, C.C., Uchiyama, H. and Ayabe, S. Catalytic specificity of pea O-methyltransferases suggests gene duplication for (+)-pisatin biosynthesis. Phytochemistry 67 (2006) 2525–2530. [DOI] [PMID: 17067644]
[EC 2.1.1.212 created 2011]
 
 
EC 2.1.1.270     
Accepted name: (+)-6a-hydroxymaackiain 3-O-methyltransferase
Reaction: S-adenosyl-L-methionine + (+)-6a-hydroxymaackiain = S-adenosyl-L-homocysteine + (+)-pisatin
Glossary: (+)-6a-hydroxymaackiain = (6aR,12aR)-6H-[1,3]dioxolo[5,6][1]benzofuro[3,2-c]chromene-3,6a(12aH)-diol
(+)-pisatin = (6aR,12aR)-3-methoxy-6H-[1,3]dioxolo[5,6][1]benzofuro[3,2-c]chromen-6a(12aH)-ol
Other name(s): HM3OMT; HMM2
Systematic name: S-adenosyl-L-methionine:(+)-6a-hydroxymaackiain 3-O-methyltransferase
Comments: The protein from the plant Pisum sativum (garden pea) methylates (+)-6a-hydroxymaackiain at the 3-position. It also methylates 2,7,4′-trihydroxyisoflavanone on the 4′-position (cf. EC 2.1.1.212, 2,7,4-trihydroxyisoflavanone 4-O-methyltransferase) with lower activity.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Preisig, C.L., Matthews, D.E. and Vanetten, H.D. Purification and characterization of S-adenosyl-L-methionine:6a-hydroxymaackiain 3-O-methyltransferase from Pisum sativum. Plant Physiol. 91 (1989) 559–566. [PMID: 16667069]
2.  Wu, Q., Preisig, C.L. and VanEtten, H.D. Isolation of the cDNAs encoding (+)6a-hydroxymaackiain 3-O-methyltransferase, the terminal step for the synthesis of the phytoalexin pisatin in Pisum sativum. Plant Mol. Biol. 35 (1997) 551–560. [PMID: 9349277]
3.  Liu, C.J., Deavours, B.E., Richard, S.B., Ferrer, J.L., Blount, J.W., Huhman, D., Dixon, R.A. and Noel, J.P. Structural basis for dual functionality of isoflavonoid O-methyltransferases in the evolution of plant defense responses. Plant Cell 18 (2006) 3656–3669. [DOI] [PMID: 17172354]
4.  Akashi, T., VanEtten, H.D., Sawada, Y., Wasmann, C.C., Uchiyama, H. and Ayabe, S. Catalytic specificity of pea O-methyltransferases suggests gene duplication for (+)-pisatin biosynthesis. Phytochemistry 67 (2006) 2525–2530. [DOI] [PMID: 17067644]
[EC 2.1.1.270 created 2013]
 
 
EC 3.5.2.20     
Accepted name: isatin hydrolase
Reaction: isatin + H2O = isatinate
Glossary: isatin = 1H-indole-2,3-dione
isatinate = 2-(2-aminophenyl)-2-oxoacetate
Systematic name: isatin amidohydrolase
Comments: Requires Mn2+. This enzyme, found in several bacterial species, is involved in the degradation of indole-3-acetic acid.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Sommer, M.R. and Jochimsen, B. Identification of enzymes involved in indole-3-acetic acid degradation. Plant Soil 186 (1996) 143–149.
2.  Bjerregaard-Andersen, K., Sommer, T., Jensen, J.K., Jochimsen, B., Etzerodt, M. and Morth, J.P. A proton wire and water channel revealed in the crystal structure of isatin hydrolase. J. Biol. Chem. 289 (2014) 21351–21359. [DOI] [PMID: 24917679]
[EC 3.5.2.20 created 2014]
 
 


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