EC |
1.1.1.291 |
Accepted name: |
2-hydroxymethylglutarate dehydrogenase |
Reaction: |
(S)-2-hydroxymethylglutarate + NAD+ = 2-formylglutarate + NADH + H+ |
|
For diagram of nicotinate catabolism, click here |
Other name(s): |
HgD |
Systematic name: |
(S)-2-hydroxymethylglutarate:NAD+ oxidoreductase |
Comments: |
NADP+ cannot replace NAD+. Forms part of the nicotinate-fermentation catabolism pathway in Eubacterium barkeri. Other enzymes involved in this pathway are EC 1.17.1.5 (nicotinate dehydrogenase), EC 1.3.7.1 (6-hydroxynicotinate reductase), EC 3.5.2.18 (enamidase), EC 5.4.99.4 (2-methyleneglutarate mutase), EC 5.3.3.6 (methylitaconate Δ-isomerase), EC 4.2.1.85 (dimethylmaleate hydratase) and EC 4.1.3.32 (2,3-dimethylmalate lyase). |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 1073478-76-8 |
References: |
1. |
Alhapel, A., Darley, D.J., Wagener, N., Eckel, E., Elsner, N. and Pierik, A.J. Molecular and functional analysis of nicotinate catabolism in Eubacterium barkeri. Proc. Natl. Acad. Sci. USA 103 (2006) 12341–12346. [DOI] [PMID: 16894175] |
|
[EC 1.1.1.291 created 2006] |
|
|
|
|
EC
|
2.8.3.7
|
Deleted entry: | succinate—citramalate CoA-transferase. The activity has now been shown to be due to two separate enzymes described by EC 2.8.3.22, succinyl-CoA—L-malate CoA-transferase, and EC 2.8.3.20, succinyl-CoA—D-citramalate CoA-transferase |
[EC 2.8.3.7 created 1972, deleted 2014] |
|
|
|
|
EC |
2.8.3.20 |
Accepted name: |
succinyl-CoA—D-citramalate CoA-transferase |
Reaction: |
(1) succinyl-CoA + (R)-citramalate = succinate + (R)-citramalyl-CoA (2) succinyl-CoA + (R)-malate = succinate + (R)-malyl-CoA
|
Glossary: |
(R)-citramalate = (2R)-2-hydroxy-2-methylbutanedioate
(R)-malate = (2R)-2-hydroxybutanedioate
(R)-malyl-CoA = (3R)-3-carboxy-3-hydroxypropanoyl-CoA |
Other name(s): |
Sct |
Systematic name: |
succinyl-CoA:(R)-citramalate CoA-transferase |
Comments: |
The enzyme, purified from the bacterium Clostridium tetanomorphum, can also accept itaconate as acceptor, with lower efficiency. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
References: |
1. |
Friedmann, S., Alber, B.E. and Fuchs, G. Properties of succinyl-coenzyme A:D-citramalate coenzyme A transferase and its role in the autotrophic 3-hydroxypropionate cycle of Chloroflexus aurantiacus. J. Bacteriol. 188 (2006) 6460–6468. [DOI] [PMID: 16952935] |
|
[EC 2.8.3.20 created 2014] |
|
|
|
|
EC |
2.8.3.22 |
Accepted name: |
succinyl-CoA—L-malate CoA-transferase |
Reaction: |
(1) succinyl-CoA + (S)-malate = succinate + (S)-malyl-CoA (2) succinyl-CoA + (S)-citramalate = succinate + (S)-citramalyl-CoA |
|
For diagram of the 3-hydroxypropanoate cycle, click here |
Glossary: |
(S)-citramalate = (2S)-2-hydroxy-2-methylbutanedioate
(S)-malate = (2S)-2-hydroxybutanedioate
(S)-malyl-CoA = (3S)-3-carboxy-3-hydroxypropanoyl-CoA |
Other name(s): |
SmtAB |
Systematic name: |
succinyl-CoA:(S)-malate CoA-transferase |
Comments: |
The enzyme, purified from the bacterium Chloroflexus aurantiacus, can also accept itaconate as acceptor, with lower efficiency. It is part of the 3-hydroxypropanoate cycle for carbon assimilation. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
References: |
1. |
Friedmann, S., Steindorf, A., Alber, B.E. and Fuchs, G. Properties of succinyl-coenzyme A:L-malate coenzyme A transferase and its role in the autotrophic 3-hydroxypropionate cycle of Chloroflexus aurantiacus. J. Bacteriol. 188 (2006) 2646–2655. [DOI] [PMID: 16547052] |
|
[EC 2.8.3.22 created 2014] |
|
|
|
|
EC |
3.5.2.18 |
Accepted name: |
enamidase |
Reaction: |
6-oxo-1,4,5,6-tetrahydronicotinate + 2 H2O = 2-formylglutarate + NH3 |
|
For diagram of nicotinate catabolism, click here |
Systematic name: |
6-oxo-1,4,5,6-tetrahydronicotinate amidohydrolase |
Comments: |
Contains iron and Zn2+. Forms part of the nicotinate-fermentation catabolism pathway in Eubacterium barkeri. Other enzymes involved in this pathway are EC 1.17.1.5 (nicotinate dehydrogenase), EC 1.3.7.1 (6-hydroxynicotinate reductase), EC 1.1.1.291 (2-hydroxymethylglutarate dehydrogenase), EC 5.4.99.4 (2-methyleneglutarate mutase), EC 5.3.3.6 (methylitaconate Δ-isomerase), EC 4.2.1.85 (dimethylmaleate hydratase) and EC 4.1.3.32 (2,3-dimethylmalate lyase). |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB |
References: |
1. |
Alhapel, A., Darley, D.J., Wagener, N., Eckel, E., Elsner, N. and Pierik, A.J. Molecular and functional analysis of nicotinate catabolism in Eubacterium barkeri. Proc. Natl. Acad. Sci. USA 103 (2006) 12341–12346. [DOI] [PMID: 16894175] |
|
[EC 3.5.2.18 created 2006] |
|
|
|
|
EC |
4.1.1.6 |
Accepted name: |
cis-aconitate decarboxylase |
Reaction: |
cis-aconitate = itaconate + CO2 |
Glossary: |
itaconate = 2-methylenesuccinate
cis-aconitate = (Z)-prop-1-ene-1,2,3-tricarboxylate |
Other name(s): |
cis-aconitic decarboxylase; cis-aconitate carboxy-lyase; CAD1 (gene name); IRG1 (gene name) |
Systematic name: |
cis-aconitate carboxy-lyase (itaconate-forming) |
Comments: |
The enzyme has been characterized from the fungus Aspergillus terreus and from human macrophages. cf. EC 4.1.1.113, trans-aconitate decarboxylase. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9025-01-8 |
References: |
1. |
Bentley, R. and Thiessen, C.P. Biosynthesis of itaconic acid in Aspergillus terreus. III. The properties and reaction mechanism of cis-aconitic acid decarboxylase. J. Biol. Chem. 226 (1957) 703–720. [PMID: 13438855] |
2. |
Dwiarti, L., Yamane, K., Yamatani, H., Kahar, P. and Okabe, M. Purification and characterization of cis-aconitic acid decarboxylase from Aspergillus terreus TN484-M1. J. Biosci. Bioeng. 94 (2002) 29–33. [PMID: 16233265] |
3. |
Kanamasa, S., Dwiarti, L., Okabe, M. and Park, E.Y. Cloning and functional characterization of the cis-aconitic acid decarboxylase (CAD) gene from Aspergillus terreus. Appl. Microbiol. Biotechnol. 80 (2008) 223–229. [PMID: 18584171] |
4. |
Michelucci, A., Cordes, T., Ghelfi, J., Pailot, A., Reiling, N., Goldmann, O., Binz, T., Wegner, A., Tallam, A., Rausell, A., Buttini, M., Linster, C.L., Medina, E., Balling, R. and Hiller, K. Immune-responsive gene 1 protein links metabolism to immunity by catalyzing itaconic acid production. Proc. Natl. Acad. Sci. USA 110 (2013) 7820–7825. [DOI] [PMID: 23610393] |
|
[EC 4.1.1.6 created 1961, modified 2018] |
|
|
|
|
EC |
4.1.1.113 |
Accepted name: |
trans-aconitate decarboxylase |
Reaction: |
trans-aconitate = itaconate + CO2 |
Glossary: |
trans-aconitate = (E)-prop-1-ene-1,2,3-tricarboxylate
itaconate = 2-methylenesuccinate |
Other name(s): |
TAD1 (gene name) |
Systematic name: |
trans-aconitate carboxy-lyase (itaconate-forming) |
Comments: |
The enzyme, characterized from the smut fungus Ustilago maydis, is involved in an alternative pathway for the biosynthesis of itaconate. cf. EC 4.1.1.6, cis-aconitate decarboxylase. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
References: |
1. |
Geiser, E., Przybilla, S.K., Friedrich, A., Buckel, W., Wierckx, N., Blank, L.M. and Bolker, M. Ustilago maydis produces itaconic acid via the unusual intermediate trans-aconitate. Microb. Biotechnol. 9 (2016) 116–126. [PMID: 26639528] |
|
[EC 4.1.1.113 created 2018] |
|
|
|
|
EC |
4.1.3.25 |
Accepted name: |
(S)-citramalyl-CoA lyase |
Reaction: |
(3S)-citramalyl-CoA = acetyl-CoA + pyruvate |
|
For diagram of the 3-hydroxypropanoate cycle, click here |
Other name(s): |
citramalyl coenzyme A lyase (ambiguous); (+)-CMA-CoA lyase; (3S)-citramalyl-CoA pyruvate-lyase; Mcl (ambiguous); citramalyl-CoA lyase (ambiguous) |
Systematic name: |
(3S)-citramalyl-CoA pyruvate-lyase (acetyl-CoA-forming) |
Comments: |
Requires Mg2+ ions for activity [3]. The enzyme from the bacterium Clostridium tetanomorphum is a component of EC 4.1.3.22, citramalate lyase [2]. It also acts on (3S)-citramalyl thioacyl-carrier protein [2]. The enzyme from the bacterium Chloroflexus aurantiacus also has the activity of EC 4.1.3.24, malyl-CoA lyase [3]. It has no activity with (3R)-citramalyl-CoA (cf. EC 4.1.3.46, (R)-citramalyl-CoA lyase) [3]. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 37290-68-9 |
References: |
1. |
Cooper, R.A. and Kornberg, H.L. The utilization of itaconate by Pseudomonas sp. Biochem. J. 91 (1964) 82–91. [PMID: 4284209] |
2. |
Dimroth, P., Buckel, W., Loyal, R. and Eggerer, H. Isolation and function of the subunits of citramalate lyase and formation of hybrids with the subunits of citrate lyase. Eur. J. Biochem. 80 (1977) 469–477. [DOI] [PMID: 923590] |
3. |
Friedmann, S., Alber, B.E. and Fuchs, G. Properties of R-citramalyl-coenzyme A lyase and its role in the autotrophic 3-hydroxypropionate cycle of Chloroflexus aurantiacus. J. Bacteriol. 189 (2007) 2906–2914. [DOI] [PMID: 17259315] |
|
[EC 4.1.3.25 created 1972, modified 2014] |
|
|
|
|
EC |
4.2.1.56 |
Accepted name: |
itaconyl-CoA hydratase |
Reaction: |
citramalyl-CoA = itaconyl-CoA + H2O |
Other name(s): |
itaconyl coenzyme A hydratase; citramalyl-CoA hydro-lyase |
Systematic name: |
citramalyl-CoA hydro-lyase (itaconyl-CoA-forming) |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 37290-83-8 |
References: |
1. |
Cooper, R.A. and Kornberg, H.L. The utilization of itaconate by Pseudomonas sp. Biochem. J. 91 (1964) 82–91. [PMID: 4284209] |
|
[EC 4.2.1.56 created 1972] |
|
|
|
|
EC |
5.3.3.6 |
Accepted name: |
methylitaconate Δ-isomerase |
Reaction: |
methylitaconate = 2,3-dimethylmaleate |
|
For diagram of nicotinate catabolism, click here |
Glossary: |
methylitaconate = 2-methylene-3-methylsuccinate |
Other name(s): |
methylitaconate isomerase |
Systematic name: |
methylitaconate Δ2-Δ3-isomerase |
Links to other databases: |
BRENDA, EXPASY, GTD, KEGG, MetaCyc, PDB, CAS registry number: 9059-08-9 |
References: |
1. |
Kung, H.-F. and Stadtman, T.C. Nicotinic acid metabolism. VI. Purification and properties of α-methyleneglutarate mutase (B12-dependent) and methylitaconate isomerase. J. Biol. Chem. 246 (1971) 3378–3388. [PMID: 5574401] |
|
[EC 5.3.3.6 created 1972] |
|
|
|
|
EC |
5.4.99.4 |
Accepted name: |
2-methyleneglutarate mutase |
Reaction: |
2-methyleneglutarate = 2-methylene-3-methylsuccinate |
|
For diagram of nicotinate catabolism, click here |
Other name(s): |
α-methyleneglutarate mutase |
Systematic name: |
2-methyleneglutarate carboxy-methylenemethylmutase |
Comments: |
Requires a cobamide cofactor. |
Links to other databases: |
BRENDA, EXPASY, GTD, KEGG, MetaCyc, CAS registry number: 9059-10-3 |
References: |
1. |
Kung, H.-F., Cederbaum, S., Tsai, L. and Stadtman, T.C. Nicotinic acid metabolism. V. A cobamide coenzyme-dependent conversion of α-methyleneglutaric acid to dimethylmaleic acid. Proc. Natl. Acad. Sci. USA 65 (1970) 978–984. [DOI] [PMID: 5266166] |
2. |
Kung, H.-F. and Stadtman, T.C. Nicotinic acid metabolism. VI. Purification and properties of α-methyleneglutarate mutase (B12-dependent) and methylitaconate isomerase. J. Biol. Chem. 246 (1971) 3378–3388. [PMID: 5574401] |
|
[EC 5.4.99.4 created 1972] |
|
|
|
|
EC |
6.2.1.4 |
Accepted name: |
succinate—CoA ligase (GDP-forming) |
Reaction: |
GTP + succinate + CoA = GDP + phosphate + succinyl-CoA |
|
For diagram of the citric-acid cycle, click here |
Other name(s): |
succinyl-CoA synthetase (GDP-forming); succinyl coenzyme A synthetase (guanosine diphosphate-forming); succinate thiokinase (ambiguous); succinic thiokinase (ambiguous); succinyl coenzyme A synthetase (ambiguous); succinate-phosphorylating enzyme (ambiguous); P-enzyme; SCS (ambiguous); G-STK; succinyl coenzyme A synthetase (GDP-forming); succinyl CoA synthetase (ambiguous) |
Systematic name: |
succinate:CoA ligase (GDP-forming) |
Comments: |
Itaconate can act instead of succinate, and ITP instead of GTP. |
Links to other databases: |
BRENDA, EXPASY, GTD, KEGG, MetaCyc, PDB, CAS registry number: 9014-36-2 |
References: |
1. |
Hager, L.P. Succinyl CoA synthetase. In: Boyer, P.D., Lardy, H. and Myrbäck, K. (Ed.), The Enzymes, 2nd edn, vol. 6, Academic Press, New York, 1962, pp. 387–399. |
2. |
Kaufman, S., Gilvarg, C., Cori, O. and Ochoa, S. Enzymatic oxidation of α-ketoglutarate and coupled phosphorylation. J. Biol. Chem. 203 (1953) 869–888. [PMID: 13084656] |
3. |
Mazumder, R., Sanadi, D.R. and Rodwell, W.V. Purification and properties of hog kidney succinic thiokinase. J. Biol. Chem. 235 (1960) 2546–2550. [PMID: 13768680] |
4. |
Sanadi, D.R., Gibson, D.M. and Ayengar, P. Guanosine triphosphate, the primary product of phosphorylation coupled to the breakdown of succinyl coenzyme A. Biochim. Biophys. Acta 14 (1954) 434–436. [DOI] [PMID: 13181903] |
|
[EC 6.2.1.4 created 1961] |
|
|
|
|