| EC |
2.3.3.5 |
| Accepted name: |
2-methylcitrate synthase |
| Reaction: |
propanoyl-CoA + H2O + oxaloacetate = (2S,3S)-2-hydroxybutane-1,2,3-tricarboxylate + CoA |
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For diagram of reaction, click here |
| Glossary: |
2-methylcitrate = (2S,3S)-2-hydroxybutane-1,2,3-tricarboxylate |
| Other name(s): |
2-methylcitrate oxaloacetate-lyase; MCS; methylcitrate synthase; methylcitrate synthetase |
| Systematic name: |
propanoyl-CoA:oxaloacetate C-propanoyltransferase (thioester-hydrolysing, 1-carboxyethyl-forming) |
| Comments: |
The enzyme acts on acetyl-CoA, propanoyl-CoA, butanoyl-CoA and pentanoyl-CoA. The relative rate of condensation of acetyl-CoA and oxaloacetate is 140% of that of propanoyl-CoA and oxaloacetate, but the enzyme is distinct from EC 2.3.3.1, citrate (Si)-synthase. Oxaloacetate cannot be replaced by glyoxylate, pyruvate or 2-oxoglutarate. |
| Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 57827-78-8 |
| References: |
| 1. |
Uchiyama, H. and Tabuchi, T. Properties of methylcitrate synthase from Candida lipolytica. Agric. Biol. Chem. 40 (1976) 1411–1418. |
| 2. |
Textor, S., Wendisch, V.F., De Graaf, A.A., Muller, U., Linder, M.I., Linder, D. and Buckel, W. Propionate oxidation in Escherichia coli: evidence for operation of a methylcitrate cycle in bacteria. Arch. Microbiol. 168 (1997) 428–436. [PMID: 9325432] |
| 3. |
Horswill, A.R. and Escalante-Semerena, J.C. Salmonella typhimurium LT2 catabolizes propionate via the 2-methylcitric acid cycle. J. Bacteriol. 181 (1999) 5615–5623. [PMID: 10482501] |
| 4. |
Brock, M., Maerker, C., Schütz, A., Völker, U. and Buckel, W. Oxidation of propionate to pyruvate in Escherichia coli. Involvement of methylcitrate dehydratase and aconitase. Eur. J. Biochem. 269 (2002) 6184–6194. [DOI] [PMID: 12473114] |
| 5. |
Domin, N., Wilson, D. and Brock, M. Methylcitrate cycle activation during adaptation of Fusarium solani and Fusarium verticillioides to propionyl-CoA-generating carbon sources. Microbiology 155 (2009) 3903–3912. [DOI] [PMID: 19661181] |
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| [EC 2.3.3.5 created 1978 as EC 4.1.3.31, transferred 2002 to EC 2.3.3.5, modified 2015] |
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EC
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4.1.3.31
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| Transferred entry: | 2-methylcitrate synthase. Now EC 2.3.3.5, 2-methylcitrate synthase
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| [EC 4.1.3.31 created 1978, deleted 2002] |
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| EC |
4.2.1.79 |
| Accepted name: |
2-methylcitrate dehydratase |
| Reaction: |
(2S,3S)-2-hydroxybutane-1,2,3-tricarboxylate = (Z)-but-2-ene-1,2,3-tricarboxylate + H2O |
| Glossary: |
(2S,3S)-2-methylcitrate = (2S,3S)-2-hydroxybutane-1,2,3-tricarboxylate
cis-2-methylaconitate = (Z)-but-2-ene-1,2,3-tricarboxylate |
| Other name(s): |
2-methylcitrate hydro-lyase; PrpD; 2-hydroxybutane-1,2,3-tricarboxylate hydro-lyase |
| Systematic name: |
(2S,3S)-2-hydroxybutane-1,2,3-tricarboxylate hydro-lyase [(Z)-but-2-ene-1,2,3-tricarboxylate-forming] |
| Comments: |
The enzyme is specific for (2S,3S)-methylcitrate, showing no activity with (2R,3S)-methylcitrate [2]. The enzyme can also use cis-aconitate as a substrate but more slowly [2]. Both this enzyme and EC 4.2.1.3, aconitate hydratase, are required to complete the isomerization of (2S,3S)-methylcitrate to (2R,3S)-2-methylisocitrate [2]. |
| Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 80891-26-5 |
| References: |
| 1. |
Aoki, H. and Tabuchi, T. Purification and properties of 2-methylcitrate dehydratase from Yarrowia lipolytica. Agric. Biol. Chem. 45 (1981) 2831–2837. |
| 2. |
Brock, M., Maerker, C., Schütz, A., Völker, U. and Buckel, W. Oxidation of propionate to pyruvate in Escherichia coli. Involvement of methylcitrate dehydratase and aconitase. Eur. J. Biochem. 269 (2002) 6184–6194. [DOI] [PMID: 12473114] |
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| [EC 4.2.1.79 created 1984] |
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| EC |
4.2.1.117 |
| Accepted name: |
2-methylcitrate dehydratase (2-methyl-trans-aconitate forming) |
| Reaction: |
(2S,3S)-2-methylcitrate = 2-methyl-trans-aconitate + H2O |
| Glossary: |
(2S,3S)-2-methylcitrate = (2S,3S)-2-hydroxybutane-1,2,3-tricarboxylate
2-methyl-trans-aconitate = (2E)-but-2-ene-1,2,3-tricarboxylate |
| Systematic name: |
(2S,3S)-2-hydroxybutane-1,2,3-tricarboxylate hydro-lyase (2-methyl-trans-aconitate-forming) |
| Comments: |
Catalyses the dehydration of (2S,3S)-2-methylcitrate, forming the trans isomer of 2-methyl-aconitate (unlike EC 4.2.1.79, which forms only the cis isomer). Part of a propionate degradation pathway. The enzyme from Shewanella oneidensis can also accept citrate and cis-aconitate, but activity with (2S,3S)-2-methylcitrate was approximately 2.5-fold higher. 2-methylisocitrate and isocitrate were not substrates [1]. An iron-sulfur protein. |
| Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
| References: |
| 1. |
Grimek, T.L. and Escalante-Semerena, J.C. The acnD genes of Shewenella oneidensis and Vibrio cholerae encode a new Fe/S-dependent 2-methylcitrate dehydratase enzyme that requires prpF function in vivo. J. Bacteriol. 186 (2004) 454–462. [DOI] [PMID: 14702315] |
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| [EC 4.2.1.117 created 2009] |
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