EC |
1.13.11.53 |
Accepted name: |
acireductone dioxygenase (Ni2+-requiring) |
Reaction: |
1,2-dihydroxy-5-(methylsulfanyl)pent-1-en-3-one + O2 = 3-(methylsulfanyl)propanoate + formate + CO |
|
For diagram of methionine salvage, click here and for diagram of reaction, click here |
Glossary: |
acireductone = 1,2-dihydroxy-5-(methylsulfanyl)pent-1-en-3-one |
Other name(s): |
ARD; 2-hydroxy-3-keto-5-thiomethylpent-1-ene dioxygenase (ambiguous); acireductone dioxygenase (ambiguous); E-2; 1,2-dihydroxy-5-(methylthio)pent-1-en-3-one:oxygen oxidoreductase (formate- and CO-forming) |
Systematic name: |
1,2-dihydroxy-5-(methylsulfanyl)pent-1-en-3-one:oxygen oxidoreductase (formate- and CO-forming) |
Comments: |
Requires Ni2+. If iron(II) is bound instead of Ni2+, the reaction catalysed by EC 1.13.11.54, acireductone dioxygenase [iron(II)-requiring], occurs instead [1]. The enzyme from the bacterium Klebsiella oxytoca (formerly Klebsiella pneumoniae) ATCC strain 8724 is involved in the methionine salvage pathway. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB |
References: |
1. |
Wray, J.W. and Abeles, R.H. A bacterial enzyme that catalyzes formation of carbon monoxide. J. Biol. Chem. 268 (1993) 21466–21469. [PMID: 8407993] |
2. |
Wray, J.W. and Abeles, R.H. The methionine salvage pathway in Klebsiella pneumoniae and rat liver. Identification and characterization of two novel dioxygenases. J. Biol. Chem. 270 (1995) 3147–3153. [DOI] [PMID: 7852397] |
3. |
Furfine, E.S. and Abeles, R.H. Intermediates in the conversion of 5′-S-methylthioadenosine to methionine in Klebsiella pneumoniae. J. Biol. Chem. 263 (1988) 9598–9606. [PMID: 2838472] |
4. |
Dai, Y., Wensink, P.C. and Abeles, R.H. One protein, two enzymes. J. Biol. Chem. 274 (1999) 1193–1195. [DOI] [PMID: 9880484] |
5. |
Mo, H., Dai, Y., Pochapsky, S.S. and Pochapsky, T.C. 1H, 13C and 15N NMR assignments for a carbon monoxide generating
metalloenzyme from Klebsiella pneumoniae. J. Biomol. NMR 14 (1999) 287–288. [PMID: 10481280] |
6. |
Dai, Y., Pochapsky, T.C. and Abeles, R.H. Mechanistic studies of two dioxygenases in the methionine salvage pathway
of Klebsiella pneumoniae. Biochemistry 40 (2001) 6379–6387. [DOI] [PMID: 11371200] |
7. |
Al-Mjeni, F., Ju, T., Pochapsky, T.C. and Maroney, M.J. XAS investigation of the structure and function of Ni in acireductone dioxygenase. Biochemistry 41 (2002) 6761–6769. [DOI] [PMID: 12022880] |
8. |
Pochapsky, T.C., Pochapsky, S.S., Ju, T., Mo, H., Al-Mjeni, F. and Maroney, M.J. Modeling and experiment yields the structure of acireductone dioxygenase from Klebsiella pneumoniae. Nat. Struct. Biol. 9 (2002) 966–972. [DOI] [PMID: 12402029] |
|
[EC 1.13.11.53 created 2006] |
|
|
|
|
EC |
1.13.11.54 |
Accepted name: |
acireductone dioxygenase [iron(II)-requiring] |
Reaction: |
1,2-dihydroxy-5-(methylsulfanyl)pent-1-en-3-one + O2 = 4-(methylsulfanyl)-2-oxobutanoate + formate |
|
For diagram of methionine salvage, click here and for diagram of reaction, click here |
Glossary: |
acireductone = 1,2-dihydroxy-5-(methylsulfanyl)pent-1-en-3-one |
Other name(s): |
ARD′; 2-hydroxy-3-keto-5-thiomethylpent-1-ene dioxygenase (ambiguous); acireductone dioxygenase (ambiguous); E-2′; E-3 dioxygenase; 1,2-dihydroxy-5-(methylthio)pent-1-en-3-one:oxygen oxidoreductase (formate-forming) |
Systematic name: |
1,2-dihydroxy-5-(methylsulfanyl)pent-1-en-3-one:oxygen oxidoreductase (formate-forming) |
Comments: |
Requires iron(II). If Ni2+ is bound instead of iron(II), the reaction catalysed by EC 1.13.11.53, acireductone dioxygenase (Ni2+-requiring), occurs instead. The enzyme from the bacterium Klebsiella oxytoca (formerly Klebsiella pneumoniae) ATCC strain 8724 is involved in the methionine salvage pathway. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB |
References: |
1. |
Wray, J.W. and Abeles, R.H. A bacterial enzyme that catalyzes formation of carbon monoxide. J. Biol. Chem. 268 (1993) 21466–21469. [PMID: 8407993] |
2. |
Wray, J.W. and Abeles, R.H. The methionine salvage pathway in Klebsiella pneumoniae and rat liver. Identification and characterization of two novel dioxygenases. J. Biol. Chem. 270 (1995) 3147–3153. [DOI] [PMID: 7852397] |
3. |
Furfine, E.S. and Abeles, R.H. Intermediates in the conversion of 5′-S-methylthioadenosine to methionine in Klebsiella pneumoniae. J. Biol. Chem. 263 (1988) 9598–9606. [PMID: 2838472] |
4. |
Dai, Y., Wensink, P.C. and Abeles, R.H. One protein, two enzymes. J. Biol. Chem. 274 (1999) 1193–1195. [DOI] [PMID: 9880484] |
5. |
Mo, H., Dai, Y., Pochapsky, S.S. and Pochapsky, T.C. 1H, 13C and 15N NMR assignments for a carbon monoxide generating
metalloenzyme from Klebsiella pneumoniae. J. Biomol. NMR 14 (1999) 287–288. [PMID: 10481280] |
6. |
Dai, Y., Pochapsky, T.C. and Abeles, R.H. Mechanistic studies of two dioxygenases in the methionine salvage pathway
of Klebsiella pneumoniae. Biochemistry 40 (2001) 6379–6387. [DOI] [PMID: 11371200] |
7. |
Al-Mjeni, F., Ju, T., Pochapsky, T.C. and Maroney, M.J. XAS investigation of the structure and function of Ni in acireductone dioxygenase. Biochemistry 41 (2002) 6761–6769. [DOI] [PMID: 12022880] |
8. |
Pochapsky, T.C., Pochapsky, S.S., Ju, T., Mo, H., Al-Mjeni, F. and Maroney, M.J. Modeling and experiment yields the structure of acireductone dioxygenase from Klebsiella pneumoniae. Nat. Struct. Biol. 9 (2002) 966–972. [DOI] [PMID: 12402029] |
|
[EC 1.13.11.54 created 2006] |
|
|
|
|
EC |
3.1.3.77 |
Accepted name: |
acireductone synthase |
Reaction: |
5-(methylsulfanyl)-2,3-dioxopentyl phosphate + H2O = 1,2-dihydroxy-5-(methylsulfanyl)pent-1-en-3-one + phosphate (overall reaction) (1a) 5-(methylsulfanyl)-2,3-dioxopentyl phosphate = 2-hydroxy-5-(methylsulfanyl)-3-oxopent-1-enyl phosphate (probably spontaneous) (1b) 2-hydroxy-5-(methylsulfanyl)-3-oxopent-1-enyl phosphate + H2O = 1,2-dihydroxy-5-(methylsulfanyl)pent-1-en-3-one + phosphate |
|
For diagram of methionine salvage, click here |
Glossary: |
acireductone = 1,2-dihydroxy-5-(methylsulfanyl)pent-1-en-3-one |
Other name(s): |
E1; E-1 enolase-phosphatase; 5-(methylthio)-2,3-dioxopentyl-phosphate phosphohydrolase (isomerizing) |
Systematic name: |
5-(methylsulfanyl)-2,3-dioxopentyl-phosphate phosphohydrolase (isomerizing) |
Comments: |
This bifunctional enzyme first enolizes the substrate to form the intermediate 2-hydroxy-5-(methylsulfanyl)-3-oxopent-1-enyl phosphate, which is then dephosphorylated to form the acireductone 1,2-dihydroxy-5-(methylsulfanyl)pent-1-en-3-one [2]. The acireductone represents a branch point in the methione-salvage pathway as it is used in the formation of formate, CO and 3-(methylsulfanyl)propanoate by EC 1.13.11.53 [acireductone dioxygenase (Ni2+-requiring)] and of formate and 4-(methylsulfanyl)-2-oxobutanoate either by a spontaneous reaction under aerobic conditions or by EC 1.13.11.54 {acireductone dioxygenase [iron(II)-requiring]} [1,2]. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB |
References: |
1. |
Myers, R.W., Wray, J.W., Fish, S. and Abeles, R.H. Purification and characterization of an enzyme involved in oxidative carbon-carbon bond cleavage reactions in the methionine salvage pathway of Klebsiella pneumoniae. J. Biol. Chem. 268 (1993) 24785–24791. [PMID: 8227039] |
2. |
Wray, J.W. and Abeles, R.H. The methionine salvage pathway in Klebsiella pneumoniae and rat liver. Identification and characterization of two novel dioxygenases. J. Biol. Chem. 270 (1995) 3147–3153. [DOI] [PMID: 7852397] |
3. |
Wang, H., Pang, H., Bartlam, M. and Rao, Z. Crystal structure of human E1 enzyme and its complex with a substrate analog reveals the mechanism of its phosphatase/enolase activity. J. Mol. Biol. 348 (2005) 917–926. [DOI] [PMID: 15843022] |
|
[EC 3.1.3.77 created 2006] |
|
|
|
|
EC |
3.1.3.87 |
Accepted name: |
2-hydroxy-3-keto-5-methylthiopentenyl-1-phosphate phosphatase |
Reaction: |
2-hydroxy-5-(methylsulfanyl)-3-oxopent-1-en-1-yl phosphate + H2O = 1,2-dihydroxy-5-(methylsulfanyl)pent-1-en-3-one + phosphate |
Other name(s): |
HK-MTPenyl-1-P phosphatase; MtnX; YkrX; 2-hydroxy-5-(methylthio)-3-oxopent-1-enyl phosphate phosphohydrolase; 2-hydroxy-5-(methylsulfanyl)-3-oxopent-1-enyl phosphate phosphohydrolase |
Systematic name: |
2-hydroxy-5-(methylsulfanyl)-3-oxopent-1-en-1-yl phosphate phosphohydrolase |
Comments: |
The enzyme participates in the methionine salvage pathway in Bacillus subtilis [2]. In some species a single bifunctional enzyme, EC 3.1.3.77, acireductone synthase, catalyses both this reaction and EC 5.3.2.5, 2,3-diketo-5-methylthiopentyl-1-phosphate enolase [1]. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB |
References: |
1. |
Myers, R.W., Wray, J.W., Fish, S. and Abeles, R.H. Purification and characterization of an enzyme involved in oxidative carbon-carbon bond cleavage reactions in the methionine salvage pathway of Klebsiella pneumoniae. J. Biol. Chem. 268 (1993) 24785–24791. [PMID: 8227039] |
2. |
Ashida, H., Saito, Y., Kojima, C., Kobayashi, K., Ogasawara, N. and Yokota, A. A functional link between RuBisCO-like protein of Bacillus and photosynthetic RuBisCO. Science 302 (2003) 286–290. [DOI] [PMID: 14551435] |
|
[EC 3.1.3.87 created 2012] |
|
|
|
|
EC |
5.3.2.5 |
Accepted name: |
2,3-diketo-5-methylthiopentyl-1-phosphate enolase |
Reaction: |
5-(methylsulfanyl)-2,3-dioxopentyl phosphate = 2-hydroxy-5-(methylsulfanyl)-3-oxopent-1-enyl phosphate |
Other name(s): |
DK-MTP-1-P enolase; MtnW; YkrW; RuBisCO-like protein; RLP; 2,3-diketo-5-methylthiopentyl-1-phosphate keto—enol-isomerase |
Systematic name: |
5-(methylsulfanyl)-2,3-dioxopentyl phosphate keto—enol-isomerase |
Comments: |
The enzyme participates in the methionine salvage pathway in Bacillus subtilis [2].In some species a single bifunctional enzyme, EC 3.1.3.77, acireductone synthase, catalyses both this reaction and EC 3.1.3.87, 2-hydroxy-3-keto-5-methylthiopentenyl-1-phosphate phosphatase [1]. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB |
References: |
1. |
Myers, R.W., Wray, J.W., Fish, S. and Abeles, R.H. Purification and characterization of an enzyme involved in oxidative carbon-carbon bond cleavage reactions in the methionine salvage pathway of Klebsiella pneumoniae. J. Biol. Chem. 268 (1993) 24785–24791. [PMID: 8227039] |
2. |
Ashida, H., Saito, Y., Kojima, C., Kobayashi, K., Ogasawara, N. and Yokota, A. A functional link between RuBisCO-like protein of Bacillus and photosynthetic RuBisCO. Science 302 (2003) 286–290. [DOI] [PMID: 14551435] |
|
[EC 5.3.2.5 created 2012] |
|
|
|
|