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Your query returned 7 entries. Printable version

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]

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]

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, PDB

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]

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]

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, PDB, 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]

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, PDB, 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]

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, PDB

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]