The Enzyme Database

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EC 1.1.1.18     
Accepted name: inositol 2-dehydrogenase
Reaction: myo-inositol + NAD+ = 2,4,6/3,5-pentahydroxycyclohexanone + NADH + H+
Other name(s): myo-inositol 2-dehydrogenase; myo-inositol:NAD+ oxidoreductase; inositol dehydrogenase; myo-inositol dehydrogenase
Systematic name: myo-inositol:NAD+ 2-oxidoreductase
Links to other databases: BRENDA, EXPASY, GTD, KEGG, MetaCyc, PDB, CAS registry number: 9028-25-5
References:
1.  Berman, T. and Magasanik, B. The pathway of myo-inositol degradation in Aerobacter aerogenes. Dehydrogenation and dehydration. J. Biol. Chem. 241 (1966) 800–806. [PMID: 5905122]
2.  Larner, J., Jackson, W.T., Graves, D.J. and Stamner, J.R. Inositol dehydrogenase from Aerobacter aerogenes. Arch. Biochem. Biophys. 60 (1956) 352–363. [DOI] [PMID: 13292912]
3.  Vidal-Lieria, M. and van Uden, N. Inositol dehydrogenase from the yeast Cryptococcus melibiosum. Biochim. Biophys. Acta 293 (1973) 295–303. [DOI] [PMID: 4351258]
[EC 1.1.1.18 created 1961]
 
 
EC 1.1.1.370     
Accepted name: scyllo-inositol 2-dehydrogenase (NAD+)
Reaction: scyllo-inositol + NAD+ = 2,4,6/3,5-pentahydroxycyclohexanone + NADH + H+
For diagram of inositol catabolism, click here
Glossary: 2,4,6/3,5-pentahydroxycyclohexanone = (2R,3S,4s,5R,6S)-2,3,4,5,6-pentahydroxycyclohexanone = scyllo-inosose
Other name(s): iolX (gene name)
Systematic name: scyllo-inositol:NAD+ 2-oxidoreductase
Comments: The enzyme, found in the bacterium Bacillus subtilis, has no activity with NADP+ [cf. EC 1.1.1.371, scyllo-inositol 2-dehydrogenase (NADP+)]. It is part of a scyllo-inositol degradation pathway leading to acetyl-CoA.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Morinaga, T., Ashida, H. and Yoshida, K. Identification of two scyllo-inositol dehydrogenases in Bacillus subtilis. Microbiology 156 (2010) 1538–1546. [DOI] [PMID: 20133360]
[EC 1.1.1.370 created 2014]
 
 
EC 1.1.1.371     
Accepted name: scyllo-inositol 2-dehydrogenase (NADP+)
Reaction: scyllo-inositol + NADP+ = 2,4,6/3,5-pentahydroxycyclohexanone + NADPH + H+
For diagram of inositol catabolism, click here
Glossary: 2,4,6/3,5-pentahydroxycyclohexanone = (2R,3S,4s,5R,6S)-2,3,4,5,6-pentahydroxycyclohexanone = scyllo-inosose
Other name(s): iolW (gene name)
Systematic name: scyllo-inositol:NADP+ 2-oxidoreductase
Comments: The enzyme, found in the bacterium Bacillus subtilis, has no activity with NAD+ [cf. EC 1.1.1.370, scyllo-inositol 2-dehydrogenase (NAD+)].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Morinaga, T., Ashida, H. and Yoshida, K. Identification of two scyllo-inositol dehydrogenases in Bacillus subtilis. Microbiology 156 (2010) 1538–1546. [DOI] [PMID: 20133360]
[EC 1.1.1.371 created 2014]
 
 
EC 2.1.1.129     
Accepted name: inositol 4-methyltransferase
Reaction: S-adenosyl-L-methionine + myo-inositol = S-adenosyl-L-homocysteine + 1D-4-O-methyl-myo-inositol
For diagram of reaction, click here
Other name(s): myo-inositol 4-O-methyltransferase; S-adenosyl-L-methionine:myo-inositol 4-O-methyltransferase; myo-inositol 6-O-methyltransferase
Systematic name: S-adenosyl-L-methionine:1D-myo-inositol 4-methyltransferase
Comments: The enzyme from the rice bean Vigna umbellata (Fabaceae) is highly specific for S-adenosyl-L-methionine. The enzyme also methylates 1L-1,2,4/3,5-cyclohexanepentol, 2,4,6/3,5-pentahydroxycyclohexanone, D,L-2,3,4,6/5-pentacyclohexanone and 2,2′-anhydro-2-C-hydroxymethyl-myo-inositol, but at lower rates than that of myo-inositol.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 169277-48-9
References:
1.  Vernon, D.M., Bohnert, H.J. A novel methyl transferase induced by osmotic stress in the facultative halophyte Mesembryanthemum crystallinum. EMBO J. 11 (1992) 2077–2085. [PMID: 1600940]
2.  Wanek, W. and Richter, A. Purification and characterization of myo-inositol 6-O-methyltransferase from Vigna umbellata Ohwi et Ohashi. Planta 197 (1995) 427–434.
[EC 2.1.1.129 created 1999 (EC 2.1.1.134 created 1999, incorporated 2002), modified 2002]
 
 
EC 2.6.1.50     
Accepted name: glutamine—scyllo-inositol transaminase
Reaction: L-glutamine + 2,4,6/3,5-pentahydroxycyclohexanone = 2-oxoglutaramate + 1-amino-1-deoxy-scyllo-inositol
Other name(s): glutamine scyllo-inosose aminotransferase; L-glutamine-keto-scyllo-inositol aminotransferase; glutamine-scyllo-inosose transaminase; L-glutamine-scyllo-inosose transaminase
Systematic name: L-glutamine:2,4,6/3,5-pentahydroxycyclohexanone aminotransferase
Comments: A pyridoxal-phosphate protein.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 9033-03-8
References:
1.  Walker, J.B. and Walker, M.S. Streptomycin biosynthesis. Transamination reactions involving inosamines and inosadiamines. Biochemistry 8 (1969) 763–770. [PMID: 5781017]
[EC 2.6.1.50 created 1972]
 
 
EC 4.2.1.44     
Accepted name: myo-inosose-2 dehydratase
Reaction: 2,4,6/3,5-pentahydroxycyclohexanone = 3,5/4-trihydroxycyclohexa-1,2-dione + H2O
For diagram of inositol catabolism, click here
Other name(s): inosose 2,3-dehydratase; ketoinositol dehydratase; 2,4,6/3,5-pentahydroxycyclohexanone hydro-lyase
Systematic name: 2,4,6/3,5-pentahydroxycyclohexanone hydro-lyase (3,5/4-trihydroxycyclohexa-1,2-dione-forming)
Comments: Requires Co2+ or Mn2+.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 37290-79-2
References:
1.  Berman, T. and Magasanik, B. The pathway of myo-inositol degradation in Aerobacter aerogenes. Dehydrogenation and dehydration. J. Biol. Chem. 241 (1966) 800–806. [PMID: 5905122]
[EC 4.2.1.44 created 1972]
 
 
EC 5.3.99.11     
Accepted name: 2-keto-myo-inositol isomerase
Reaction: 2,4,6/3,5-pentahydroxycyclohexanone = 2D-2,3,5/4,6-pentahydroxycyclohexanone
For diagram of inositol catabolism, click here
Glossary: 2,4,6/3,5-pentahydroxycyclohexanone = (2R,3S,4s,5R,6S)-2,3,4,5,6-pentahydroxycyclohexanone = scyllo-inosose
Other name(s): IolI; inosose isomerase; 2KMI isomerase.
Systematic name: 2,4,6/3,5-pentahydroxycyclohexanone 2-isomerase
Comments: Requires a divalent metal ion for activity. Mn2+, Fe2+ and Co2+ can be used. The enzyme, found in the bacterium Bacillus subtilis, is part of the myo-inositol/D-chiro-inositol degradation pathway leading to acetyl-CoA.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Zhang, R.G., Dementieva, I., Duke, N., Collart, F., Quaite-Randall, E., Alkire, R., Dieckman, L., Maltsev, N., Korolev, O. and Joachimiak, A. Crystal structure of Bacillus subtilis ioli shows endonuclase IV fold with altered Zn binding. Proteins 48 (2002) 423–426. [DOI] [PMID: 12112707]
2.  Yoshida, K., Yamaguchi, M., Morinaga, T., Ikeuchi, M., Kinehara, M. and Ashida, H. Genetic modification of Bacillus subtilis for production of D-chiro-inositol, an investigational drug candidate for treatment of type 2 diabetes and polycystic ovary syndrome. Appl. Environ. Microbiol. 72 (2006) 1310–1315. [DOI] [PMID: 16461681]
[EC 5.3.99.11 created 2014]
 
 


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