The Enzyme Database

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EC 5.4.1.1     
Accepted name: lysolecithin acylmutase
Reaction: 2-lysolecithin = 3-lysolecithin
Other name(s): lysolecithin migratase
Systematic name: lysolecithin 2,3-acylmutase
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 9031-24-7
References:
1.  Uziel, M. and Hanahan, D.J. An enzyme-catalyzed acyl migration: a lysolecithin migratase. J. Biol. Chem. 226 (1957) 789–798. [PMID: 13438864]
[EC 5.4.1.1 created 1961]
 
 
EC 5.4.1.2      
Transferred entry: precorrin-8X methylmutase. Now EC 5.4.99.61, precorrin-8X methylmutase
[EC 5.4.1.2 created 1999, deleted 2014]
 
 
EC 5.4.1.3     
Accepted name: 2-methylfumaryl-CoA isomerase
Reaction: 2-methylfumaryl-CoA = 3-methylfumaryl-CoA
For diagram of the 3-hydroxypropanoate cycle, click here
Glossary: 2-methylfumaryl-CoA = (E)-3-carboxy-2-methylprop-2-enoyl-CoA
3-methylfumaryl-CoA = (E)-3-carboxybut-2-enoyl-CoA
Other name(s): mesaconyl-CoA C1-C4 CoA transferase; Mct
Systematic name: 2-methylfumaryl-CoA 1,4-CoA-mutase
Comments: The enzyme, purified from the bacterium Chloroflexus aurantiacus, acts as an intramolecular CoA transferase and does not transfer CoA to free mesaconate. It is part of the 3-hydroxypropanoate cycle for carbon assimilation.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB
References:
1.  Zarzycki, J., Brecht, V., Muller, M. and Fuchs, G. Identifying the missing steps of the autotrophic 3-hydroxypropionate CO2 fixation cycle in Chloroflexus aurantiacus. Proc. Natl. Acad. Sci. USA 106 (2009) 21317–21322. [DOI] [PMID: 19955419]
[EC 5.4.1.3 created 2014]
 
 
EC 5.4.1.4     
Accepted name: D-galactarolactone isomerase
Reaction: D-galactaro-1,5-lactone = D-galactaro-1,4-lactone
Other name(s): GLI
Systematic name: D-galactaro-1,5-lactone isomerase (D-galactaro-1,4-lactone-forming)
Comments: The enzyme, characterized from the bacterium Agrobacterium fabrum strain C58, belongs to the amidohydrolase superfamily. It participates in the degradation of D-galacturonate.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB
References:
1.  Bouvier, J.T., Groninger-Poe, F.P., Vetting, M., Almo, S.C. and Gerlt, J.A. Galactaro δ-lactone isomerase: lactone isomerization by a member of the amidohydrolase superfamily. Biochemistry 53 (2014) 614–616. [DOI] [PMID: 24450804]
[EC 5.4.1.4 created 2015]
 
 
EC 5.4.2.1      
Transferred entry: phosphoglycerate mutase. Now recognized as two separate enzymes EC 5.4.2.11, phosphoglycerate mutase (2,3-diphosphoglycerate-dependent) and EC 5.4.2.12, phosphoglycerate mutase (2,3-diphosphoglycerate-independent)
[EC 5.4.2.1 created 1961 (EC 2.7.5.3 created 1961, incorporated 1984), deleted 2013]
 
 
EC 5.4.2.2     
Accepted name: phosphoglucomutase (α-D-glucose-1,6-bisphosphate-dependent)
Reaction: α-D-glucose 1-phosphate = D-glucose 6-phosphate
For diagram of UDP-glucose, UDP-galactose and UDP-glucuronate biosynthesis, click here
Other name(s): glucose phosphomutase (ambiguous); phosphoglucose mutase (ambiguous)
Systematic name: α-D-glucose 1,6-phosphomutase
Comments: Maximum activity is only obtained in the presence of α-D-glucose 1,6-bisphosphate. This bisphosphate is an intermediate in the reaction, being formed by transfer of a phosphate residue from the enzyme to the substrate, but the dissociation of bisphosphate from the enzyme complex is much slower than the overall isomerization. The enzyme also catalyses (more slowly) the interconversion of 1-phosphate and 6-phosphate isomers of many other α-D-hexoses, and the interconversion of α-D-ribose 1-phosphate and 5-phosphate. cf. EC 5.4.2.5, phosphoglucomutase (glucose-cofactor).
Links to other databases: BRENDA, EXPASY, GTD, KEGG, MetaCyc, PDB, CAS registry number: 9001-81-4
References:
1.  Joshi, J.G. and Handler, P. Phosphoglucomutase. I. Purification and properties of phosphoglucomutase from Escherichia coli. J. Biol. Chem. 239 (1964) 2741–2751. [PMID: 14216423]
2.  Najjar, V.A. Phosphoglucomutase. In: Boyer, P.D., Lardy, H. and Myrbäck, K. (Ed.), The Enzymes, 2nd edn, vol. 6, Academic Press, New York, 1962, pp. 161–178.
3.  Ray, W.J. and Roscelli, G.A. A kinetic study of the phosphoglucomutase pathway. J. Biol. Chem. 239 (1964) 1228–1236. [PMID: 14165931]
4.  Ray, W.J., Jr. and Peck, E.J., Jr. Phosphomutases. In: Boyer, P.D. (Ed.), The Enzymes, 3rd edn, vol. 6, 1972, pp. 407–477.
5.  Sutherland, E.W., Cohn, M., Posternak, T. and Cori, C.F. The mechanism of the phosphoglucomutase reaction. J. Biol. Chem. 180 (1949) 1285–1295. [PMID: 18148026]
[EC 5.4.2.2 created 1961 as EC 2.7.5.1, transferred 1984 to EC 5.4.2.2]
 
 
EC 5.4.2.3     
Accepted name: phosphoacetylglucosamine mutase
Reaction: N-acetyl-α-D-glucosamine 1-phosphate = N-acetyl-D-glucosamine 6-phosphate
For diagram of UDP-N-acetylglucosamine biosynthesis, click here
Other name(s): acetylglucosamine phosphomutase; acetylglucosamine phosphomutase; acetylaminodeoxyglucose phosphomutase; phospho-N-acetylglucosamine mutase; N-acetyl-D-glucosamine 1,6-phosphomutase
Systematic name: N-acetyl-α-D-glucosamine 1,6-phosphomutase
Comments: The enzyme is activated by N-acetyl-α-D-glucosamine 1,6-bisphosphate.
Links to other databases: BRENDA, EXPASY, GTD, KEGG, MetaCyc, PDB, CAS registry number: 9027-51-4
References:
1.  Carlson, D.M. Phosphoacetylglucosamine mutase from pig submaxillary gland. Methods Enzymol. 8 (1966) 179–182.
2.  Leloir, L.F. and Cardini, C.E. Enzymes acting on glucosamine phosphates. Biochim. Biophys. Acta 20 (1956) 33–42. [PMID: 13315346]
3.  Ray, W.J., Jr. and Peck, E.J., Jr. Phosphomutases. In: Boyer, P.D. (Ed.), The Enzymes, 3rd edn, vol. 6, 1972, pp. 407–477.
4.  Reissig, J.L. and Leloir, L.F. Phosphoacetylglucosamine mutase from Neurospora. Methods Enzymol. 8 (1966) 175–178.
[EC 5.4.2.3 created 1961 as EC 2.7.5.2, transferred 1984 to EC 5.4.2.3]
 
 
EC 5.4.2.4     
Accepted name: bisphosphoglycerate mutase
Reaction: 3-phospho-D-glyceroyl phosphate = 2,3-bisphospho-D-glycerate
Other name(s): diphosphoglycerate mutase; glycerate phosphomutase; bisphosphoglycerate synthase; bisphosphoglyceromutase; biphosphoglycerate synthase; diphosphoglyceric mutase; 2,3-diphosphoglycerate mutase; phosphoglyceromutase; 2,3-diphosphoglycerate synthase; DPGM; 2,3-bisphosphoglycerate mutase; BPGM; diphosphoglyceromutase; 2,3-diphosphoglyceromutase
Systematic name: 3-phospho-D-glycerate 1,2-phosphomutase
Comments: In the direction shown, this enzyme is phosphorylated by 3-phosphoglyceroyl phosphate, to give phosphoenzyme and 3-phosphoglycerate. The latter is rephosphorylated by the enzyme to yield 2,3-bisphosphoglycerate, but this reaction is slowed by dissociation of 3-phosphoglycerate from the enzyme, which is therefore more active in the presence of added 3-phosphoglycerate. This enzyme also catalyses, slowly, the reaction of EC 5.4.2.11 [phosphoglycerate mutase (2,3-diphosphoglycerate-dependent)] and EC 5.4.2.12 [phosphoglycerate mutase (2,3-diphosphoglycerate-independent)].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 37211-69-1
References:
1.  Ray, W.J., Jr. and Peck, E.J., Jr. Phosphomutases. In: Boyer, P.D. (Ed.), The Enzymes, 3rd edn, vol. 6, 1972, pp. 407–477.
2.  Rose, Z.B. The purification and properties of diphosphoglycerate mutase from human erythrocytes. J. Biol. Chem. 243 (1968) 4810–4820. [PMID: 5687724]
3.  Rose, Z.B. The enzymology of 2,3-bisphosphoglycerate. Adv. Enzymol. Relat. Areas Mol. Biol. 51 (1980) 211–253. [PMID: 6255773]
[EC 5.4.2.4 created 1961 as EC 2.7.5.4, transferred 1984 to EC 5.4.2.4]
 
 
EC 5.4.2.5     
Accepted name: phosphoglucomutase (glucose-cofactor)
Reaction: α-D-glucose 1-phosphate = D-glucose 6-phosphate
Other name(s): glucose phosphomutase (ambiguous); glucose-1-phosphate phosphotransferase
Systematic name: α-D-glucose 1,6-phosphomutase (glucose-cofactor)
Comments: The enzyme is activated by D-glucose, which probably acts as an acceptor for a phosphate residue from the substrate, thus being itself converted into the product. cf. EC 5.4.2.2, phosphoglucomutase (α-D-glucose-1,6-bisphosphate-dependent).
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 37278-22-1
References:
1.  Fujimoto, A., Ingram, P. and Smith, R.A. D-Glucose-1-phosphate:D-glucose-6-phosphotransferase. Biochim. Biophys. Acta 96 (1965) 91–101. [DOI] [PMID: 14285271]
2.  Ray, W.J., Jr. and Peck, E.J., Jr. Phosphomutases. In: Boyer, P.D. (Ed.), The Enzymes, 3rd edn, vol. 6, 1972, pp. 407–477.
[EC 5.4.2.5 created 1972 as EC 2.7.5.5, transferred 1984 to EC 5.4.2.5]
 
 
EC 5.4.2.6     
Accepted name: β-phosphoglucomutase
Reaction: β-D-glucose 1-phosphate = β-D-glucose 6-phosphate
For diagram of reaction, click here
Other name(s): β-pgm (gene name)
Systematic name: β-D-glucose 1,6-phosphomutase
Comments: The enzyme requires Mg2+ and phosphorylation of an aspartate residue at the active site. The enzyme is able to autophosphorylate itself with its substrate β-D-glucose 1-phosphate. Although this is a slow reaction, only a single turnover is required for activation. Once the phosphorylated enzyme is formed, it generates the reaction intermediate β-D-glucose 1,6-bisphosphate, which can be used to phosphorylate the enzyme in subsequent cycles [4]. cf. EC 5.4.2.2, phosphoglucomutase (α-D-glucose-1,6-bisphosphate-dependent).
Links to other databases: BRENDA, EXPASY, GTD, KEGG, MetaCyc, PDB, CAS registry number: 68651-99-0
References:
1.  Ben-Zvi, R. and Schramm, M. A phosphoglucomutase specific for β-glucose 1-phosphate. J. Biol. Chem. 236 (1961) 2186–2189.
2.  Ray, W.J., Jr. and Peck, E.J., Jr. Phosphomutases. In: Boyer, P.D. (Ed.), The Enzymes, 3rd edn, vol. 6, 1972, pp. 407–477.
3.  Lahiri, S.D., Zhang, G., Dunaway-Mariano, D. and Allen, K.N. The pentacovalent phosphorus intermediate of a phosphoryl transfer reaction. Science 299 (2003) 2067–2071. [DOI] [PMID: 12637673]
4.  Dai, J., Wang, L., Allen, K.N., Radstrom, P. and Dunaway-Mariano, D. Conformational cycling in β-phosphoglucomutase catalysis: reorientation of the β-D-glucose 1,6-(Bis)phosphate intermediate. Biochemistry 45 (2006) 7818–7824. [DOI] [PMID: 16784233]
[EC 5.4.2.6 created 1984]
 
 
EC 5.4.2.7     
Accepted name: phosphopentomutase
Reaction: α-D-ribose 1-phosphate = D-ribose 5-phosphate
Other name(s): phosphodeoxyribomutase; deoxyribose phosphomutase; deoxyribomutase; phosphoribomutase; α-D-glucose-1,6-bisphosphate:deoxy-D-ribose-1-phosphate phosphotransferase; D-ribose 1,5-phosphomutase
Systematic name: α-D-ribose 1,5-phosphomutase
Comments: Also converts 2-deoxy-α-D-ribose 1-phosphate into 2-deoxy-D-ribose 5-phosphate. α-D-Ribose 1,5-bisphosphate, 2-deoxy-α-D-ribose 1,5-bisphosphate, or α-D-glucose 1,6-bisphosphate can act as cofactor.
Links to other databases: BRENDA, EXPASY, GTD, KEGG, MetaCyc, PDB, CAS registry number: 9026-77-1
References:
1.  Hammen-Jepersen, K. and Munch-Petersen, A. Phosphodeoxyribomutase from Escherichia coli. Purification and some properties. Eur. J. Biochem. 17 (1970) 397–407. [DOI] [PMID: 4992818]
2.  Kammen, H.O. and Koo, R. Phosphopentomutases. I. Identification of two activities in rabbit tissues. J. Biol. Chem. 244 (1969) 4888–4893. [PMID: 5824563]
3.  Ray, W.J., Jr. and Peck, E.J., Jr. Phosphomutases. In: Boyer, P.D. (Ed.), The Enzymes, 3rd edn, vol. 6, 1972, pp. 407–477.
[EC 5.4.2.7 created 1972 as EC 2.7.5.6, transferred 1984 to EC 5.4.2.7]
 
 
EC 5.4.2.8     
Accepted name: phosphomannomutase
Reaction: α-D-mannose 1-phosphate = D-mannose 6-phosphate
For diagram of GDP-L-fucose and GDP-mannose biosynthesis, click here
Other name(s): mannose phosphomutase; phosphomannose mutase; D-mannose 1,6-phosphomutase
Systematic name: α-D-mannose 1,6-phosphomutase
Comments: α-D-Mannose 1,6-bisphosphate or α-D-glucose 1,6-bisphosphate can act as cofactor.
Links to other databases: BRENDA, EXPASY, GTD, KEGG, MetaCyc, PDB, CAS registry number: 59536-73-1
References:
1.  Small, D.M. and Matheson, N.K. Phosphomannomutase and phosphoglucomutase in developing Cassia corymbosa seeds. Phytochemistry 18 (1979) 1147–1150.
[EC 5.4.2.8 created 1981 as EC 2.7.5.7, transferred 1984 to EC 5.4.2.8]
 
 
EC 5.4.2.9     
Accepted name: phosphoenolpyruvate mutase
Reaction: phosphoenolpyruvate = 3-phosphonopyruvate
For diagram of reaction, click here
Other name(s): phosphoenolpyruvate-phosphonopyruvate phosphomutase; PEP phosphomutase; phosphoenolpyruvate phosphomutase; PEPPM; PEP phosphomutase
Systematic name: phosphoenolpyruvate 2,3-phosphonomutase
Comments: Involved in the biosynthesis of the C-P bond, although the equilibrium greatly favours phosphoenolpyruvate.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 115756-49-5
References:
1.  Bowman, E., McQueney, M., Barry, R.J. and Dunaway-Mariano, D. Catalysis and thermodynamics of the phosphoenolpyruvate phosphonopyruvate rearrangement - entry into the phosphonate class of naturally-occurring organo-phosphorus compounds. J. Am. Chem. Soc. 110 (1988) 5575–5576.
2.  Hikada, T., Imai, S., Hara, O., Anzai, H., Murakami, T., Nagaoka, K. and Seto, H. Carboxyphosphonoenolpyruvate phosphonomutase, a novel enzyme catalyzing C-P bond formation. J. Bacteriol. 172 (1990) 3066–3072. [DOI] [PMID: 2160937]
3.  Seidel, H.M., Freeman, S. and Knowles, J.R. Phosphonate biosynthesis: isolation of the enzyme responsible for the formation of a carbon-phosphorus bond. Nature 335 (1988) 457–458. [DOI] [PMID: 3138545]
[EC 5.4.2.9 created 1990]
 
 
EC 5.4.2.10     
Accepted name: phosphoglucosamine mutase
Reaction: α-D-glucosamine 1-phosphate = D-glucosamine 6-phosphate
For diagram of the biosynthesis of UDP-N-acetylglucosamine, click here
Systematic name: α-D-glucosamine 1,6-phosphomutase
Comments: The enzyme is involved in the pathway for bacterial cell-wall peptidoglycan and lipopolysaccharide biosyntheses, being an essential step in the pathway for UDP-N-acetylglucosamine biosynthesis. The enzyme from Escherichia coli is activated by phosphorylation and can be autophosphorylated in vitro by α-D-glucosamine 1,6-bisphosphate, which is an intermediate in the reaction, α-D-glucose 1,6-bisphosphate or ATP. It can also catalyse the interconversion of α-D-glucose 1-phosphate and glucose 6-phosphate, although at a much lower rate.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9031-92-9
References:
1.  Mengin-Lecreulx, D. and van Heijenoort, J. Characterization of the essential gene glmM encoding phosphoglucosamine mutase in Escherichia coli. J. Biol. Chem. 271 (1996) 32–39. [DOI] [PMID: 8550580]
2.  de Reuse, H., Labigne, A. and Mengin-Lecreulx, D. The Helicobacter pylori ureC gene codes for a phosphoglucosamine mutase. J. Bacteriol. 179 (1997) 3488–3493. [DOI] [PMID: 9171391]
3.  Jolly, L., Wu, S., van Heijenoort, J., de Lencastre, H., Mengin-Lecreulx, D. and Tomas, A. The femR315 gene from Staphylococcus aureus, the interruption of which results in reduced methicillin resistance, encodes a phosphoglucosamine mutase. J. Bacteriol. 179 (1997) 5321–5325. [DOI] [PMID: 9286983]
4.  Jolly, L., Ferrari, P., Blanot, D., van Heijenoort, J., Fassy, F. and Mengin-Lecreulx, D. Reaction mechanism of phosphoglucosamine mutase from Escherichia coli. Eur. J. Biochem. 262 (1999) 202–210. [DOI] [PMID: 10231382]
5.  Jolly, L., Pompeo, F., van Heijenoort, J., Fassy, F. and Mengin-Lecreulx, D. Autophosphorylation of phosphoglucosamine mutase from Escherichia coli. J. Bacteriol. 182 (2000) 1280–1285. [DOI] [PMID: 10671448]
[EC 5.4.2.10 created 2001]
 
 
EC 5.4.2.11     
Accepted name: phosphoglycerate mutase (2,3-diphosphoglycerate-dependent)
Reaction: 2-phospho-D-glycerate = 3-phospho-D-glycerate (overall reaction)
(1a) [enzyme]-L-histidine + 2,3-bisphospho-D-glycerate = [enzyme]-Nτ-phospho-L-histidine + 2/3-phospho-D-glycerate
(1b) [enzyme]-Nτ-phospho-L-histidine + 2-phospho-D-glycerate = [enzyme]-L-histidine + 2,3-bisphospho-D-glycerate
(1c) [enzyme]-L-histidine + 2,3-bisphospho-D-glycerate = [enzyme]-Nτ-phospho-L-histidine + 3-phospho-D-glycerate
(1d) [enzyme]-Nτ-phospho-L-histidine + 2/3-bisphospho-D-glycerate = [enzyme]-L-histidine + 2,3-bisphospho-D-glycerate
For diagram of the Entner-Doudoroff pathway, click here
Glossary: 2/3-phospho-D-glycerate = 2-phospho-D-glycerate or 3-phospho-D-glycerate
Other name(s): glycerate phosphomutase (diphosphoglycerate cofactor); 2,3-diphosphoglycerate dependent phosphoglycerate mutase; cofactor dependent phosphoglycerate mutase; phosphoglycerate phosphomutase (ambiguous); phosphoglyceromutase (ambiguous); monophosphoglycerate mutase (ambiguous); monophosphoglyceromutase (ambiguous); GriP mutase (ambiguous); PGA mutase (ambiguous); MPGM; PGAM; PGAM-d; PGM; dPGM
Systematic name: D-phosphoglycerate 2,3-phosphomutase (2,3-diphosphoglycerate-dependent)
Comments: The enzymes from vertebrates, platyhelminths, mollusks, annelids, crustaceans, insects, algae, some fungi and some bacteria (particularly Gram-negative) require 2,3-bisphospho-D-glycerate as a cofactor. The enzyme is activated by 2,3-bisphospho-D-glycerate by transferring a phosphate to histidine (His10 in man and Escherichia coli, His8 in Saccharomyces cerevisiae). This phosphate can be transferred to the free OH of 2-phospho-D-glycerate, followed by transfer of the phosphate already on the phosphoglycerate back to the histidine. cf. EC 5.4.2.12 phosphoglycerate mutase. The enzyme has no requirement for metal ions. This enzyme also catalyse, slowly, the reactions of EC 5.4.2.4 bisphosphoglycerate mutase.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB
References:
1.  Grisolia, S. Phosphoglyceric acid mutase. Methods Enzymol. 5 (1962) 236–242.
2.  Ray, W.J., Jr. and Peck, E.J., Jr. Phosphomutases. In: Boyer, P.D. (Ed.), The Enzymes, 3rd edn, vol. 6, 1972, pp. 407–477.
3.  Rose, Z.B. The enzymology of 2,3-bisphosphoglycerate. Adv. Enzymol. Relat. Areas Mol. Biol. 51 (1980) 211–253. [PMID: 6255773]
4.  Rigden, D.J., Walter, R.A., Phillips, S.E. and Fothergill-Gilmore, L.A. Sulphate ions observed in the 2.12 Å structure of a new crystal form of S. cerevisiae phosphoglycerate mutase provide insights into understanding the catalytic mechanism. J. Mol. Biol. 286 (1999) 1507–1517. [DOI] [PMID: 10064712]
5.  Bond, C.S., White, M.F. and Hunter, W.N. High resolution structure of the phosphohistidine-activated form of Escherichia coli cofactor-dependent phosphoglycerate mutase. J. Biol. Chem. 276 (2001) 3247–3253. [DOI] [PMID: 11038361]
6.  Rigden, D.J., Mello, L.V., Setlow, P. and Jedrzejas, M.J. Structure and mechanism of action of a cofactor-dependent phosphoglycerate mutase homolog from Bacillus stearothermophilus with broad specificity phosphatase activity. J. Mol. Biol. 315 (2002) 1129–1143. [DOI] [PMID: 11827481]
7.  Rigden, D.J., Littlejohn, J.E., Henderson, K. and Jedrzejas, M.J. Structures of phosphate and trivanadate complexes of Bacillus stearothermophilus phosphatase PhoE: structural and functional analysis in the cofactor-dependent phosphoglycerate mutase superfamily. J. Mol. Biol. 325 (2003) 411–420. [DOI] [PMID: 12498792]
[EC 5.4.2.11 created 1961 as EC 5.4.2.1 (EC 2.7.5.3 created 1961, incorporated 1984) transferred 2013 to EC 5.4.2.11, modified 2014]
 
 
EC 5.4.2.12     
Accepted name: phosphoglycerate mutase (2,3-diphosphoglycerate-independent)
Reaction: 2-phospho-D-glycerate = 3-phospho-D-glycerate
For diagram of the Entner-Doudoroff pathway, click here
Other name(s): cofactor independent phosphoglycerate mutase; 2,3-diphosphoglycerate-independent phosphoglycerate mutase; phosphoglycerate phosphomutase (ambiguous); phosphoglyceromutase (ambiguous); monophosphoglycerate mutase (ambiguous); monophosphoglyceromutase (ambiguous); GriP mutase (ambiguous); PGA mutase (ambiguous); iPGM; iPGAM; PGAM-i
Systematic name: D-phosphoglycerate 2,3-phosphomutase (2,3-diphosphoglycerate-independent)
Comments: The enzymes from higher plants, algae, some fungi, nematodes, sponges, coelenterates, myriapods, arachnids, echinoderms, archaea and some bacteria (particularly Gram-positive) have maximum activity in the absence of 2,3-bisphospho-D-glycerate. cf. EC 5.4.2.11 phosphoglycerate mutase (2,3-diphosphoglycerate-dependent). The enzyme contains two Mn2+ (or in some species two Co2+ ions). The reaction involves a phosphotransferase reaction to serine followed by transfer back to the glycerate at the other position. Both metal ions are involved in the reaction.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB
References:
1.  Jedrzejas, M.J., Chander, M., Setlow, P. and Krishnasamy, G. Mechanism of catalysis of the cofactor-independent phosphoglycerate mutase from Bacillus stearothermophilus. Crystal structure of the complex with 2-phosphoglycerate. J. Biol. Chem. 275 (2000) 23146–23153. [DOI] [PMID: 10764795]
2.  Rigden, D.J., Lamani, E., Mello, L.V., Littlejohn, J.E. and Jedrzejas, M.J. Insights into the catalytic mechanism of cofactor-independent phosphoglycerate mutase from X-ray crystallography, simulated dynamics and molecular modeling. J. Mol. Biol. 328 (2003) 909–920. [DOI] [PMID: 12729763]
3.  Zhang, Y., Foster, J.M., Kumar, S., Fougere, M. and Carlow, C.K. Cofactor-independent phosphoglycerate mutase has an essential role in Caenorhabditis elegans and is conserved in parasitic nematodes. J. Biol. Chem. 279 (2004) 37185–37190. [DOI] [PMID: 15234973]
4.  Nukui, M., Mello, L.V., Littlejohn, J.E., Setlow, B., Setlow, P., Kim, K., Leighton, T. and Jedrzejas, M.J. Structure and molecular mechanism of Bacillus anthracis cofactor-independent phosphoglycerate mutase: a crucial enzyme for spores and growing cells of Bacillus species. Biophys J 92 (2007) 977–988. [DOI] [PMID: 17085493]
5.  Nowicki, M.W., Kuaprasert, B., McNae, I.W., Morgan, H.P., Harding, M.M., Michels, P.A., Fothergill-Gilmore, L.A. and Walkinshaw, M.D. Crystal structures of Leishmania mexicana phosphoglycerate mutase suggest a one-metal mechanism and a new enzyme subclass. J. Mol. Biol. 394 (2009) 535–543. [DOI] [PMID: 19781556]
6.  Mercaldi, G.F., Pereira, H.M., Cordeiro, A.T., Michels, P.A. and Thiemann, O.H. Structural role of the active-site metal in the conformation of Trypanosoma brucei phosphoglycerate mutase. FEBS J. 279 (2012) 2012–2021. [DOI] [PMID: 22458781]
[EC 5.4.2.12 created 2013]
 
 
EC 5.4.2.13     
Accepted name: phosphogalactosamine mutase
Reaction: D-galactosamine 6-phosphate = α-D-galactosamine-1-phosphate
For diagram of UDP-N-acetylglucosamine biosynthesis, click here
Other name(s): ST0242 (locus name)
Systematic name: α-D-galactosamine 1,6-phosphomutase
Comments: The enzyme, characterized from the archaeon Sulfolobus tokodaii, is also active toward D-glucosamine 6-phosphate (cf. EC 5.4.2.10, phosphoglucosamine mutase).
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB
References:
1.  Dadashipour, M., Iwamoto, M., Hossain, M.M., Akutsu, J.I., Zhang, Z. and Kawarabayasi, Y. Identification of a direct biosynthetic pathway for UDP-N-acetylgalactosamine from glucosamine-6-phosphate in thermophilic crenarchaeon Sulfolobus tokodaii. J. Bacteriol. 200 (2018) . [PMID: 29507091]
[EC 5.4.2.13 created 2018]
 
 
EC 5.4.3.1      
Deleted entry:  ornithine 4,5-aminomutase. This reaction was due to a mixture of EC 5.1.1.12 (ornithine racemase) and EC 5.4.3.5 (D-ornithine 4,5-aminomutase)
[EC 5.4.3.1 created 1972, deleted 1976]
 
 
EC 5.4.3.2     
Accepted name: lysine 2,3-aminomutase
Reaction: L-lysine = (3S)-3,6-diaminohexanoate
For diagram of lysine catabolism, click here
Systematic name: L-lysine 2,3-aminomutase
Comments: This enzyme is a member of the ’AdoMet radical’ (radical SAM) family. It contains pyridoxal phosphate and a [4Fe-4S] cluster and binds an exchangeable S-adenosyl-L-methionine molecule. Activity in vitro requires a strong reductant such as dithionite and strictly anaerobic conditions. A 5′-deoxyadenosyl radical is generated during the reaction cycle by reductive cleavage of S-adenosyl-L-methionine, mediated by the iron-sulfur cluster. S-adenosyl-L-methionine is regenerated at the end of the reaction.
Links to other databases: BRENDA, EXPASY, GTD, KEGG, MetaCyc, PDB, CAS registry number: 9075-20-1
References:
1.  Zappia, V. and Barker, H.A. Studies on lysine-2,3-aminomutase. Subunit structure and sulfhydryl groups. Biochim. Biophys. Acta 207 (1970) 505–513. [DOI] [PMID: 5452674]
2.  Aberhart, D.J., Lim, H.-J. and Weiller, B.H. Stereochemistry of lysine 2,3-aminomutase. J. Am. Chem. Soc. 103 (1981) 6750–6752.
3.  Frey, P.A. Lysine 2,3-aminomutase: is adenosylmethionine a poor man’s adenosylcobalamin. FASEB J. 7 (1993) 662–670. [PMID: 8500691]
4.  Lieder, K.W., Booker, S., Ruzicka, F.J., Beinert, H., Reed, G.H. and Frey, P.A. S-Adenosylmethionine-dependent reduction of lysine 2,3-aminomutase and observation of the catalytically functional iron-sulfur centers by electron paramagnetic resonance. Biochemistry 37 (1998) 2578–2585. [DOI] [PMID: 9485408]
5.  Lepore, B.W., Ruzicka, F.J., Frey, P.A. and Ringe, D. The x-ray crystal structure of lysine-2,3-aminomutase from Clostridium subterminale. Proc. Natl. Acad. Sci. USA 102 (2005) 13819–13824. [DOI] [PMID: 16166264]
6.  Frey, P.A. and Reed, G.H. Pyridoxal-5′-phosphate as the catalyst for radical isomerization in reactions of PLP-dependent aminomutases. Biochim. Biophys. Acta 1814 (2011) 1548–1557. [DOI] [PMID: 21435400]
[EC 5.4.3.2 created 1972]
 
 
EC 5.4.3.3     
Accepted name: lysine 5,6-aminomutase
Reaction: (1) (3S)-3,6-diaminohexanoate = (3S,5S)-3,5-diaminohexanoate
(2) D-lysine = (2R,5S)-2,5-diaminohexanoate
For diagram of lysine catabolism, click here
Other name(s): β-lysine 5,6-aminomutase; β-lysine mutase; L-β-lysine 5,6-aminomutase; D-lysine 5,6-aminomutase; D-α-lysine mutase; adenosylcobalamin-dependent D-lysine 5,6-aminomutase
Systematic name: (3S)-3,6-diaminohexanoate 5,6-aminomutase
Comments: This enzyme is a member of the ‘AdoMet radical’ (radical SAM) family. It requires pyridoxal 5′-phosphate and adenosylcobalamin for activity. A 5′-deoxyadenosyl radical is generated during the reaction cycle by reductive cleavage of adenosylcobalamin, which is regenerated at the end of the reaction.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9075-69-8
References:
1.  Stadtman, T.C. and Tasi, L. A cobamide coenzyme dependent migration of the ε-amino group of D-lysine. Biochem. Biophys. Res. Commun. 28 (1967) 920–926. [DOI] [PMID: 4229021]
2.  Stadtman, T.C. and Renz, P. Anaerobic degradation of lysine. V. Some properties of the cobamide coenzyme-dependent β-lysine mutase of Clostridium sticklandii. Arch. Biochem. Biophys. 125 (1968) 226–239. [DOI] [PMID: 5649516]
3.  Morley, C.G.D. and Stadtman, T.C. Studies on the fermentation of D-α-lysine. Purification and properties of an adenosine triphosphate regulated B12-coenzyme-dependent D-α-lysine mutase complex from Clostridium sticklandii. Biochemistry 9 (1970) 4890–4900. [PMID: 5480154]
4.  Retey, J., Kunz, F., Arigoni, D. and Stadtman, T.C. Zur Kenntnis der β-Lysin-Mutase-Reaktion: mechanismus und sterischer Verlauf. Helv. Chim. Acta 61 (1978) 2989–2998.
5.  Chang, C.H. and Frey, P.A. Cloning, sequencing, heterologous expression, purification, and characterization of adenosylcobalamin-dependent D-lysine 5, 6-aminomutase from Clostridium sticklandii. J. Biol. Chem. 275 (2000) 106–114. [DOI] [PMID: 10617592]
6.  Tang, K.H., Harms, A. and Frey, P.A. Identification of a novel pyridoxal 5′-phosphate binding site in adenosylcobalamin-dependent lysine 5,6-aminomutase from Porphyromonas gingivalis. Biochemistry 41 (2002) 8767–8776. [DOI] [PMID: 12093296]
7.  Tang, K.H., Mansoorabadi, S.O., Reed, G.H. and Frey, P.A. Radical triplets and suicide inhibition in reactions of 4-thia-D- and 4-thia-L-lysine with lysine 5,6-aminomutase. Biochemistry 48 (2009) 8151–8160. [DOI] [PMID: 19634897]
8.  Berkovitch, F., Behshad, E., Tang, K.H., Enns, E.A., Frey, P.A. and Drennan, C.L. A locking mechanism preventing radical damage in the absence of substrate, as revealed by the x-ray structure of lysine 5,6-aminomutase. Proc. Natl. Acad. Sci. USA 101 (2004) 15870–15875. [DOI] [PMID: 15514022]
[EC 5.4.3.3 created 1972 (EC 5.4.3.4 created 1972, incorporated 2017), modified 2017]
 
 
EC 5.4.3.4      
Transferred entry: D-lysine 5,6-aminomutase. Now included in EC 5.4.3.3, lysine 5,6-aminomutase
[EC 5.4.3.4 created 1972, modified 2003, deleted 2017]
 
 
EC 5.4.3.5     
Accepted name: D-ornithine 4,5-aminomutase
Reaction: D-ornithine = (2R,4S)-2,4-diaminopentanoate
Other name(s): D-α-ornithine 5,4-aminomutase; D-ornithine aminomutase
Systematic name: D-ornithine 4,5-aminomutase
Comments: A pyridoxal-phosphate protein that requires a cobamide cofactor for activity.
Links to other databases: BRENDA, EXPASY, GTD, KEGG, MetaCyc, PDB, CAS registry number: 62213-30-3
References:
1.  Somack, R. and Costilow, R.N. Purification and properties of a pyridoxal phosphate and coenzyme B12 dependent D-α-ornithine 5,4-aminomutase. Biochemistry 12 (1973) 2597–2604. [PMID: 4711468]
[EC 5.4.3.5 created 1972 as EC 5.4.3.1, transferred 1976 to EC 5.4.3.5, modified 2003]
 
 
EC 5.4.3.6     
Accepted name: tyrosine 2,3-aminomutase
Reaction: L-tyrosine = 3-amino-3-(4-hydroxyphenyl)propanoate
Other name(s): tyrosine α,β-mutase
Systematic name: L-tyrosine 2,3-aminomutase
Comments: Requires ATP.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9073-38-5
References:
1.  Kurylo-Borowska, Z. and Abramsky, T. Biosynthesis of β-tyrosine. Biochim. Biophys. Acta 264 (1972) 1–10. [DOI] [PMID: 5021987]
[EC 5.4.3.6 created 1976]
 
 
EC 5.4.3.7     
Accepted name: leucine 2,3-aminomutase
Reaction: (2S)-α-leucine = (3R)-β-leucine
Systematic name: (2S)-α-leucine 2,3-aminomutase
Comments: Requires a cobamide cofactor.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 59125-53-0
References:
1.  Freer, I., Pedrocchi-Fantoni, G., Picken, D.J. and Overton, K.H. Stereochemistry of the leucine 2,3-aminomutase from tissue-cultures of Andrographis paniculata. J. Chem. Soc. Chem. Commun. (1981) 80–82.
2.  Poston, J.M. Leucine 2,3-aminomutase, an enzyme of leucine catabolism. J. Biol. Chem. 251 (1976) 1859–1863. [PMID: 1270414]
3.  Poston, J.M. Coenzyme B12-dependent enzymes in potatoes: leucine 2,3-aminomutase and methylmalonyl-CoA mutase. Phytochemistry 17 (1978) 401–402.
[EC 5.4.3.7 created 1982]
 
 
EC 5.4.3.8     
Accepted name: glutamate-1-semialdehyde 2,1-aminomutase
Reaction: L-glutamate 1-semialdehyde = 5-aminolevulinate
For diagram of the early stages of porphyrin biosynthesis, click here and for mechanism of reaction, click here
Glossary: L-glutamate 1-semialdehyde = (S)-4-amino-5-oxopentanoate
Other name(s): glutamate-1-semialdehyde aminotransferase
Systematic name: (S)-4-amino-5-oxopentanoate 4,5-aminomutase
Comments: Requires pyridoxal phosphate.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 68518-07-0
References:
1.  Gough, S.P. and Kannangara, C.G. Biosynthesis of δ-aminolevulinate in greening barley leaves: glutamate 1-semialdehyde aminotransferase. Carlsberg Res. Commun. 43 (1978) 185–194.
[EC 5.4.3.8 created 1983]
 
 
EC 5.4.3.9     
Accepted name: glutamate 2,3-aminomutase
Reaction: L-glutamate = 3-aminopentanedioate
Glossary: 3-aminopentanedioate = isoglutamate
Systematic name: L-glutamate 2,3-aminomutase
Comments: This enzyme is a member of the ’AdoMet radical’ (radical SAM) family. It contains pyridoxal phosphate and a [4Fe-4S] cluster, which is coordinated by 3 cysteines and binds an exchangeable S-adenosyl-L-methionine molecule. During the reaction cycle, the AdoMet forms a 5′-deoxyadenosyl radical, which is regenerated at the end of the reaction.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Ruzicka, F.J. and Frey, P.A. Glutamate 2,3-aminomutase: a new member of the radical SAM superfamily of enzymes. Biochim. Biophys. Acta 1774 (2007) 286–296. [DOI] [PMID: 17222594]
[EC 5.4.3.9 created 2012]
 
 
EC 5.4.3.10     
Accepted name: phenylalanine aminomutase (L-β-phenylalanine forming)
Reaction: L-phenylalanine = L-β-phenylalanine
Glossary: L-β-phenylalanine = (R)-3-amino-3-phenylpropanoate
Systematic name: L-phenylalanine 2,3-aminomutase [(R)-3-amino-3-phenylpropanoate-forming]
Comments: The enzyme contains the cofactor 3,5-dihydro-5-methylidene-4H-imidazol-4-one (MIO). This unique cofactor is formed autocatalytically by cyclization and dehydration of the three amino-acid residues alanine, serine and glycine. cf. EC 5.4.3.11, phenylalanine aminomutase (D-β-phenylalanine forming).
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB
References:
1.  Feng, L., Wanninayake, U., Strom, S., Geiger, J. and Walker, K.D. Mechanistic, mutational, and structural evaluation of a Taxus phenylalanine aminomutase. Biochemistry 50 (2011) 2919–2930. [DOI] [PMID: 21361343]
[EC 5.4.3.10 created 2013]
 
 
EC 5.4.3.11     
Accepted name: phenylalanine aminomutase (D-β-phenylalanine forming)
Reaction: L-phenylalanine = D-β-phenylalanine
Glossary: D-β-phenylalanine = (S)-3-amino-3-phenylpropanoate
Other name(s): admH (gene name); L-phenylalanine 2,3-aminomutase [(S)-3-amino-3-phenylpropanoate]
Systematic name: L-phenylalanine 2,3-aminomutase [(S)-3-amino-3-phenylpropanoate-forming]
Comments: The enzyme from the bacterium Pantoea agglomerans produces D-β-phenylalanine, an intermediate in the biosynthesis of the polyketide non-ribosomal antibiotic andrimid. The enzyme contains the cofactor 3,5-dihydro-5-methylidene-4H-imidazol-4-one (MIO), which is formed autocatalytically by cyclization and dehydration of the three amino-acid residues alanine, serine and glycine. cf. EC 5.4.3.10, phenylalanine aminomutase (L-β-phenylalanine forming).
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Ratnayake, N.D., Wanninayake, U., Geiger, J.H. and Walker, K.D. Stereochemistry and mechanism of a microbial phenylalanine aminomutase. J. Am. Chem. Soc. 133 (2011) 8531–8533. [DOI] [PMID: 21561099]
[EC 5.4.3.11 created 2013]
 
 
EC 5.4.4.1     
Accepted name: (hydroxyamino)benzene mutase
Reaction: (hydroxyamino)benzene = 2-aminophenol
Other name(s): HAB mutase; hydroxylaminobenzene hydroxymutase; hydroxylaminobenzene mutase
Systematic name: (hydroxyamino)benzene hydroxymutase
Links to other databases: BRENDA, EAWAG-BBD, EXPASY, KEGG, MetaCyc, CAS registry number: 261765-91-7
References:
1.  He, Z., Nadeau, L.J. and Spain, J.C. Characterization of hydroxylaminobenzene mutase from pNBZ139 cloned from Pseudomonas pseudoalcaligenes JS45: a highly-associated sodium-dodecyl-sulfate-stable enzyme catalyzing an intramolecular transfer of hydroxyl group. Eur. J. Biochem. 267 (2000) 1110–1116. [DOI] [PMID: 10672020]
2.  Davis, J.K., Paoli, G.C., He, Z., Nadeau, L.J., Somerville, C.C. and Spain, J.C. Sequence analysis and initial characterization of two isozymes of hydroxylaminobenzene mutase from Pseudomonas pseudoalcaligenes JS45. Appl. Environ. Microbiol. 66 (2000) 2965–2971. [DOI] [PMID: 10877793]
[EC 5.4.4.1 created 2003]
 
 
EC 5.4.4.2     
Accepted name: isochorismate synthase
Reaction: chorismate = isochorismate
For diagram of shikimate and chorismate biosynthesis, click here
Other name(s): MenF
Systematic name: isochorismate hydroxymutase
Comments: Requires Mg2+. The reaction is reversible.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 37318-53-9
References:
1.  Young, I.G. and Gibson, F. Regulation of the enzymes involved in the biosynthesis of 2,3-dihydroxybenzoic acid in Aerobacter aerogenes and Escherichia coli. Biochim. Biophys. Acta 177 (1969) 401–411. [DOI] [PMID: 4306838]
2.  van Tegelen, L.J., Moreno, P.R., Croes, A.F., Verpoorte, R. and Wullems, G.J. Purification and cDNA cloning of isochorismate synthase from elicited cell cultures of Catharanthus roseus. Plant Physiol. 119 (1999) 705–712. [PMID: 9952467]
3.  Dahm, C., Müller, R., Schulte, G., Schmidt, K. and Leistner, E. The role of isochorismate hydroxymutase genes entC and menF in enterobactin and menaquinone biosynthesis in Escherichia coli. Biochim. Biophys. Acta 1425 (1998) 377–386. [DOI] [PMID: 9795253]
4.  Daruwala, R., Kwon, O., Meganathan, R. and Hudspeth, M.E. A new isochorismate synthase specifically involved in menaquinone (vitamin K2) biosynthesis encoded by the menF gene. FEMS Microbiol. Lett. 140 (1996) 159–163. [PMID: 8764478]
[EC 5.4.4.2 created 1972 as EC 5.4.99.6, transferred 2003 to EC 5.4.4.2]
 
 
EC 5.4.4.3     
Accepted name: 3-(hydroxyamino)phenol mutase
Reaction: 3-hydroxyaminophenol = aminohydroquinone
Other name(s): 3-hydroxylaminophenol mutase; 3HAP mutase
Systematic name: 3-(hydroxyamino)phenol hydroxymutase
Links to other databases: BRENDA, EAWAG-BBD, EXPASY, KEGG, MetaCyc, CAS registry number: 224427-05-8
References:
1.  Schenzle, A., Lenke, H., Spain, J.C. and Knackmuss, H.J. 3-Hydroxylaminophenol mutase from Ralstonia eutropha JMP134 catalyzes a Bamberger rearrangement. J. Bacteriol. 181 (1999) 1444–1450. [PMID: 10049374]
[EC 5.4.4.3 created 2003]
 
 
EC 5.4.4.4     
Accepted name: geraniol isomerase
Reaction: geraniol = (3S)-linalool
For diagram of acyclic monoterpenoid biosynthesis, click here
Systematic name: geraniol hydroxymutase
Comments: In absence of oxygen the bifunctional linalool dehydratase-isomerase can catalyse in vitro two reactions, the isomerization of (3S)-linalool to geraniol and the hydration of myrcene to (3S)-linalool, the latter activity being classified as EC 4.2.1.127, linalool dehydratase.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB
References:
1.  Brodkorb, D., Gottschall, M., Marmulla, R., Lüddeke, F. and Harder, J. Linalool dehydratase-isomerase, a bifunctional enzyme in the anaerobic degradation of monoterpenes. J. Biol. Chem. 285 (2010) 30436–30442. [DOI] [PMID: 20663876]
2.  Lüddeke, F. and Harder, J. Enantiospecific (S)-(+)-linalool formation from β-myrcene by linalool dehydratase-isomerase. Z. Naturforsch. C 66 (2011) 409–412. [PMID: 21950166]
[EC 5.4.4.4 created 2011, modified 2012]
 
 
EC 5.4.4.5     
Accepted name: 9,12-octadecadienoate 8-hydroperoxide 8R-isomerase
Reaction: (8R,9Z,12Z)-8-hydroperoxyoctadeca-9,12-dienoate = (5S,8R,9Z,12Z)-5,8-dihydroxyoctadeca-9,12-dienoate
Other name(s): 5,8-LDS (bifunctional enzyme); 5,8-linoleate diol synthase (bifunctional enzyme); 8-hydroperoxide isomerase; (8R,9Z,12Z)-8-hydroperoxy-9,12-octadecadienoate mutase ((5S,8R,9Z,12Z)-5,8-dihydroxy-9,12-octadecadienoate-forming); PpoA
Systematic name: (8R,9Z,12Z)-8-hydroperoxyoctadeca-9,12-dienoate hydroxymutase [(5S,8R,9Z,12Z)-5,8-dihydroxyoctadeca-9,12-dienoate-forming]
Comments: The enzyme contains heme [3]. The bifunctional enzyme from Aspergillus nidulans uses different heme domains to catalyse two separate reactions. Linoleic acid is oxidized within the N-terminal heme peroxidase domain to (8R,9Z,12Z)-8-hydroperoxyoctadeca-9,12-dienoate (cf. EC 1.13.11.60, linoleate 8R-lipoxygenase), which is subsequently isomerized to (5S,8R,9Z,12Z)-5,8-dihydroxyoctadeca-9,12-dienoate within the C-terminal P-450 heme thiolate domain [3].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Hoffmann, I., Jerneren, F., Garscha, U. and Oliw, E.H. Expression of 5,8-LDS of Aspergillus fumigatus and its dioxygenase domain. A comparison with 7,8-LDS, 10-dioxygenase, and cyclooxygenase. Arch. Biochem. Biophys. 506 (2011) 216–222. [DOI] [PMID: 21130068]
2.  Jerneren, F., Garscha, U., Hoffmann, I., Hamberg, M. and Oliw, E.H. Reaction mechanism of 5,8-linoleate diol synthase, 10R-dioxygenase, and 8,11-hydroperoxide isomerase of Aspergillus clavatus. Biochim. Biophys. Acta 1801 (2010) 503–507. [DOI] [PMID: 20045744]
3.  Brodhun, F., Gobel, C., Hornung, E. and Feussner, I. Identification of PpoA from Aspergillus nidulans as a fusion protein of a fatty acid heme dioxygenase/peroxidase and a cytochrome P450. J. Biol. Chem. 284 (2009) 11792–11805. [DOI] [PMID: 19286665]
[EC 5.4.4.5 created 2011]
 
 
EC 5.4.4.6     
Accepted name: 9,12-octadecadienoate 8-hydroperoxide 8S-isomerase
Reaction: (8R,9Z,12Z)-8-hydroperoxyoctadeca-9,12-dienoate = (7S,8S,9Z,12Z)-7,8-dihydroxyoctadeca-9,12-dienoate
Other name(s): 8-hydroperoxide isomerase (ambiguous); (8R,9Z,12Z)-8-hydroperoxy-9,12-octadecadienoate mutase ((7S,8S,9Z,12Z)-7,8-dihydroxy-9,12-octadecadienoate-forming)
Systematic name: (8R,9Z,12Z)-8-hydroperoxyoctadeca-9,12-dienoate hydroxymutase [(7S,8S,9Z,12Z)-7,8-dihydroxyoctadeca-9,12-dienoate-forming]
Comments: The enzyme contains heme. The bifunctional enzyme from Gaeumannomyces graminis catalyses the oxidation of linoleic acid to (8R,9Z,12Z)-8-hydroperoxyoctadeca-9,12-dienoate (cf. EC 1.13.11.60, linoleate 8R-lipoxygenase), which is then isomerized to (7S,8S,9Z,12Z)-5,8-dihydroxyoctadeca-9,12-dienoate [3].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Hamberg, M., Zhang, L.-Y., Brodowsky, I.D. and Oliw, E.H. Sequential oxygenation of linoleic acid in the fungus Gaeumannomyces graminis: stereochemistry of dioxygenase and hydroperoxide isomerase reactions. Arch. Biochem. Biophys. 309 (1994) 77–80. [DOI] [PMID: 8117115]
2.  Su, C., Sahlin, M. and Oliw, E.H. A protein radical and ferryl intermediates are generated by linoleate diol synthase, a ferric hemeprotein with dioxygenase and hydroperoxide isomerase activities. J. Biol. Chem. 273 (1998) 20744–20751. [DOI] [PMID: 9694817]
3.  Su, C. and Oliw, E.H. Purification and characterization of linoleate 8-dioxygenase from the fungus Gaeumannomyces graminis as a novel hemoprotein. J. Biol. Chem. 271 (1996) 14112–14118. [DOI] [PMID: 8662736]
[EC 5.4.4.6 created 2011]
 
 
EC 5.4.4.7     
Accepted name: hydroperoxy icosatetraenoate isomerase
Reaction: a hydroperoxyicosatetraenoate = a hydroxyepoxyicosatrienoate
Glossary: (12R)-HPETE = (5Z,8Z,10E,12R,14Z)-12-hydroperoxyicosa-5,8,10,14-tetraenoate
(8S)-HPETE = (5Z,8S,9E,11Z,14Z)-8-hydroperoxyicosa-5,9,11,14-tetraenoate
Other name(s): epidermal lipoxygenase-3 (ambiguous); eLOX3 (ambiguous)
Systematic name: hydroperoxyicosatetraenoate hydroxymutase
Comments: Binds Fe2+. The enzyme from mammals accepts a range of hydroperoxyicosatetraenoates producing one or several different hydroxyepoxyicosatrienoates. The human enzyme has highest activity with (12R)-HPETE producing (5Z,8R,9E,11R,12R,14Z)-8-hydroxy-11,12-epoxyicosa-5,9,14-trienoate, followed by (12S)-HPETE producing (5Z,8Z,10R,11S,12S,14Z)-10-hydroxy-11,12-epoxyicosa-5,8,14-trienoate and (5Z,8R,9E,11S,12S,14Z)-8-hydroxy-11,12-epoxyicosa-5,9,14-trienoate [1]. The mouse enzyme has highest activity with (8S)-HPETE, producing (5Z,8S,9S,10R,11Z,14Z)-10-hydroxy-8,9-epoxyicosa-5,11,14-trienoate [2]. The enzymes also have the activity of EC 4.2.1.152, hydroperoxy icosatetraenoate dehydratase.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB
References:
1.  Yu, Z., Schneider, C., Boeglin, W.E., Marnett, L.J. and Brash, A.R. The lipoxygenase gene ALOXE3 implicated in skin differentiation encodes a hydroperoxide isomerase. Proc. Natl. Acad. Sci. USA 100 (2003) 9162–9167. [DOI] [PMID: 12881489]
2.  Yu, Z., Schneider, C., Boeglin, W.E. and Brash, A.R. Human and mouse eLOX3 have distinct substrate specificities: implications for their linkage with lipoxygenases in skin. Arch. Biochem. Biophys. 455 (2006) 188–196. [DOI] [PMID: 17045234]
3.  Zheng, Y. and Brash, A.R. Dioxygenase activity of epidermal lipoxygenase-3 unveiled: typical and atypical features of its catalytic activity with natural and synthetic polyunsaturated fatty acids. J. Biol. Chem. 285 (2010) 39866–39875. [DOI] [PMID: 20921226]
[EC 5.4.4.7 created 2014]
 
 
EC 5.4.4.8     
Accepted name: linalool isomerase
Reaction: (RS)-linalool = geraniol
For diagram of acyclic monoterpenoid biosynthesis, click here
Other name(s): 3,1-hydroxyl-Δ12-mutase (linalool isomerase)
Systematic name: (RS)-linalool hydroxymutase
Comments: Isolated from the bacterium Thauera linaloolentis grown on (RS)-linalool as the sole source of carbon. Unlike EC 5.4.4.4, geraniol isomerase, which only acts on (S)-linalool, this enzyme acts equally well on both enantiomers.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Marmulla, R., Šafarić, B., Markert, S., Schweder, T. and Harder, J. Linalool isomerase, a membrane-anchored enzyme in the anaerobic monoterpene degradation in Thauera linaloolentis 47Lol. BMC Biochem. 17:6 (2016). [DOI] [PMID: 26979141]
[EC 5.4.4.8 created 2017]
 
 
EC 5.4.99.1     
Accepted name: methylaspartate mutase
Reaction: L-threo-3-methylaspartate = L-glutamate
Other name(s): glutamate mutase; glutamic mutase; glutamic isomerase; glutamic acid mutase; glutamic acid isomerase; methylaspartic acid mutase; β-methylaspartate-glutamate mutase; glutamate isomerase
Systematic name: L-threo-3-methylaspartate carboxy-aminomethylmutase
Comments: Requires a cobamide cofactor.
Links to other databases: BRENDA, EXPASY, GTD, KEGG, MetaCyc, PDB, CAS registry number: 9032-97-7
References:
1.  Barker, H.A., Rooze, V., Suzuki, F. and Iodice, A.A. The glutamate mutase system. Assays and properties. J. Biol. Chem. 239 (1964) 3260–3266. [PMID: 14245371]
2.  Weissbach, H., Toohey, J. and Barker, H.A. Isolation and properties of B12 coenzymes containing benzimidazole or dimethylbenzimidazole. Proc. Natl. Acad. Sci. USA 45 (1959) 521–528. [DOI] [PMID: 16590408]
[EC 5.4.99.1 created 1961]
 
 
EC 5.4.99.2     
Accepted name: methylmalonyl-CoA mutase
Reaction: (R)-methylmalonyl-CoA = succinyl-CoA
For diagram of the 3-hydroxypropanoate cycle, click here
Other name(s): methylmalonyl-CoA CoA-carbonyl mutase; methylmalonyl coenzyme A mutase; methylmalonyl coenzyme A carbonylmutase; (S)-methylmalonyl-CoA mutase; (R)-2-methyl-3-oxopropanoyl-CoA CoA-carbonylmutase [incorrect]
Systematic name: (R)-methylmalonyl-CoA CoA-carbonylmutase
Comments: Requires a cobamide coenzyme.
Links to other databases: BRENDA, EAWAG-BBD, EXPASY, GTD, KEGG, MetaCyc, PDB, CAS registry number: 9023-90-9
References:
1.  Barker, H.A. Coenzyme B12-dependent mutases causing carbon chain rearrangements. In: Boyer, P.D. (Ed.), The Enzymes, 3rd edn, vol. 6, Academic Press, New York, 1972, pp. 509–537.
[EC 5.4.99.2 created 1961, modified 1983]
 
 
EC 5.4.99.3     
Accepted name: 2-acetolactate mutase
Reaction: 2-acetolactate = 3-hydroxy-3-methyl-2-oxobutanoate
Other name(s): acetolactate mutase; acetohydroxy acid isomerase
Systematic name: 2-acetolactate methylmutase
Comments: Requires ascorbic acid; also converts 2-aceto-2-hydroxybutanoate to 3-hydroxy-3-methyl-2-oxopentanoate.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 37318-52-8
References:
1.  Allaudeen, H.S. and Ramakrishnan, T. Biosynthesis of isoleucine and valine in Mycobacterium tuberculosis H37 Rv. Arch. Biochem. Biophys. 125 (1968) 199–209. [DOI] [PMID: 4384955]
[EC 5.4.99.3 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 5.4.99.5     
Accepted name: chorismate mutase
Reaction: chorismate = prephenate
For diagram of phenylalanine and tyrosine biosynthesis, click here and for mechanism of reaction, click here
Other name(s): hydroxyphenylpyruvate synthase
Systematic name: chorismate pyruvatemutase
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9068-30-8
References:
1.  Cotton, R.G.H. and Gibson, F. The biosynthesis of phenylalanine and tyrosine; enzymes converting chorismic acid into prephenic acid and their relationships to prephenate dehydratase and prephenate dehydrogenase. Biochim. Biophys. Acta 100 (1965) 76–88. [DOI] [PMID: 14323651]
2.  Lorence, J.H. and Nester, E.W. Multiple molecular forms of chorismate mutase in Bacillus subtillis. Biochemistry 6 (1967) 1541–1543. [PMID: 4962500]
3.  Sprössler, B. and Lingens, F. Chorismat-Mutase aus Claviceps. I. Eigenschaften der Chorismat-Mutase aus verschiedenen Claviceps-Stämmen. Hoppe-Seyler's Z. Physiol. Chem. 351 (1970) 448–458. [PMID: 5443801]
4.  Woodin, T.S. and Nishioka, L. Evidence for three isozymes of chorismate mutase in alfalfa. Biochim. Biophys. Acta 309 (1973) 211–223. [DOI] [PMID: 4708674]
[EC 5.4.99.5 created 1972]
 
 
EC 5.4.99.6      
Transferred entry: isochorismate synthase. Now EC 5.4.4.2, isochorismate synthase
[EC 5.4.99.6 created 1972, deleted 2003]
 
 
EC 5.4.99.7     
Accepted name: lanosterol synthase
Reaction: (3S)-2,3-epoxy-2,3-dihydrosqualene = lanosterol
For diagram of lanosterol and cycloartenol biosynthesis, click here
Other name(s): 2,3-epoxysqualene lanosterol cyclase; squalene-2,3-oxide-lanosterol cyclase; lanosterol 2,3-oxidosqualene cyclase; squalene 2,3-epoxide:lanosterol cyclase; 2,3-oxidosqualene sterol cyclase; oxidosqualene cyclase; 2,3-oxidosqualene cyclase; 2,3-oxidosqualene-lanosterol cyclase; oxidosqualene-lanosterol cyclase; squalene epoxidase-cyclase; (S)-2,3-epoxysqualene mutase (cyclizing, lanosterol-forming)
Systematic name: (3S)-2,3-epoxy-2,3-dihydrosqualene mutase (cyclizing, lanosterol-forming)
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9032-71-7
References:
1.  Dean, P.D.G., Oritz de Montellano, P.R., Bloch, K. and Corey, E.J. A soluble 2,3-oxidosqualene sterol cyclase. J. Biol. Chem. 242 (1967) 3014–3015. [PMID: 6027261]
[EC 5.4.99.7 created 1961 as EC 1.99.1.13, transferred 1965 to EC 1.14.1.3, part transferred 1972 to EC 5.4.99.7 rest to EC 1.14.99.7]
 
 
EC 5.4.99.8     
Accepted name: cycloartenol synthase
Reaction: (3S)-2,3-epoxy-2,3-dihydrosqualene = cycloartenol
For diagram of lanosterol and cycloartenol biosynthesis, click here
Other name(s): 2,3-epoxysqualene cycloartenol-cyclase; squalene-2,3-epoxide-cycloartenol cyclase; 2,3-epoxysqualene-cycloartenol cyclase; 2,3-oxidosqualene-cycloartenol cyclase; (S)-2,3-epoxysqualene mutase (cyclizing, cycloartenol-forming)
Systematic name: (3S)-2,3-epoxy-2,3-dihydrosqualene mutase (cyclizing, cycloartenol-forming)
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 9075-25-6
References:
1.  Rees, H.H., Goad, L.J. and Goodwin, T.W. 2,3-Oxidosqualene cycloartenol cyclase from Ochromonas malhamensis. Biochim. Biophys. Acta 176 (1969) 892–894. [DOI] [PMID: 5797101]
[EC 5.4.99.8 created 1972]
 
 
EC 5.4.99.9     
Accepted name: UDP-galactopyranose mutase
Reaction: UDP-α-D-galactopyranose = UDP-α-D-galactofuranose
For diagram of UDP-glucose, UDP-galactose and UDP-glucuronate biosynthesis, click here
Other name(s): UGM; UDP-D-galactopyranose furanomutase
Systematic name: UDP-α-D-galactopyranose furanomutase
Comments: A flavoenzyme which generates UDP-α-D-glactofuranose required for cell wall formation in bacteria, fungi, and protozoa.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 174632-18-9
References:
1.  Trejo, A.G., Chittenden, G.J.F., Buchanan, J.G. and Baddiley, J. Uridine diphosphate α-D-galactofuranose, an intermediate in the biosynthesis of galactofuranosyl residues. Biochem. J. 117 (1970) 637–639. [PMID: 5419754]
2.  Karunan Partha, S., Bonderoff, S.A., van Straaten, K.E. and Sanders, D.A. Expression, purification and preliminary X-ray crystallographic analysis of UDP-galactopyranose mutase from Deinococcus radiodurans. Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun. 65 (2009) 843–845. [DOI] [PMID: 19652355]
3.  Dhatwalia, R., Singh, H., Oppenheimer, M., Karr, D.B., Nix, J.C., Sobrado, P. and Tanner, J.J. Crystal structures and small-angle x-ray scattering analysis of UDP-galactopyranose mutase from the pathogenic fungus Aspergillus fumigatus. J. Biol. Chem. 287 (2012) 9041–9051. [DOI] [PMID: 22294687]
4.  van Straaten, K.E., Routier, F.H. and Sanders, D.A. Towards the crystal structure elucidation of eukaryotic UDP-galactopyranose mutase. Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun. 68 (2012) 455–459. [DOI] [PMID: 22505419]
[EC 5.4.99.9 created 1984, modified 2012]
 
 
EC 5.4.99.10      
Deleted entry: isomaltulose synthetase. Now included with EC 5.4.99.11, isomaltulose synthase
[EC 5.4.99.10 created 1984, deleted 1992]
 
 
EC 5.4.99.11     
Accepted name: isomaltulose synthase
Reaction: sucrose = 6-O-α-D-glucopyranosyl-D-fructofuranose
Other name(s): isomaltulose synthetase; sucrose α-glucosyltransferase; trehalulose synthase
Systematic name: sucrose glucosylmutase
Comments: The enzyme simultaneously produces isomaltulose (6-O-α-D-glucopyranosyl-D-fructose) and smaller amounts of trehalulose (1-O-α-D-glucopyranosyl-β-D-fructose) from sucrose.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 159940-49-5
References:
1.  Cheetham, P.S.J. The extraction and mechanism of a novel isomaltulose-synthesizing enzyme from Erwinia rhapontici. Biochem. J. 220 (1984) 213–220. [PMID: 6743261]
2.  Cheetham, P.S.J., Imber, C.E. and Isherwood, J. The formation of isomaltulose by immobilized Erwinia rhapontici. Nature 299 (1982) 628–631.
[EC 5.4.99.11 created 1989 (EC 5.4.99.10 created 1984, incorporated 1992)]
 
 
EC 5.4.99.12     
Accepted name: tRNA pseudouridine38-40 synthase
Reaction: tRNA uridine38-40 = tRNA pseudouridine38-40
Other name(s): TruA; tRNA pseudouridine synthase I; PSUI; hisT (gene name)
Systematic name: tRNA-uridine38-40 uracil mutase
Comments: The uridylate residues at positions 38, 39 and 40 of nearly all tRNAs are isomerized to pseudouridine. TruA specifically modifies uridines at positions 38, 39, and/or 40 in the anticodon stem loop of tRNAs with highly divergent sequences and structures [1].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 61506-89-6
References:
1.  Hur, S. and Stroud, R.M. How U38, 39, and 40 of many tRNAs become the targets for pseudouridylation by TruA. Mol. Cell 26 (2007) 189–203. [DOI] [PMID: 17466622]
2.  Huang, L., Pookanjanatavip, M., Gu, X. and Santi, D.V. A conserved aspartate of tRNA pseudouridine synthase is essential for activity and a probable nucleophilic catalyst. Biochemistry 37 (1998) 344–351. [DOI] [PMID: 9425056]
3.  Kammen, H.O., Marvel, C.C., Hardy, L. and Penhoet, E.E. Purification, structure, and properties of Escherichia coli tRNA pseudouridine synthase I. J. Biol. Chem. 263 (1988) 2255–2263. [PMID: 3276686]
4.  Turnbough, C.L., Jr., Neill, R.J., Landsberg, R. and Ames, B.N. Pseudouridylation of tRNAs and its role in regulation in Salmonella typhimurium. J. Biol. Chem. 254 (1979) 5111–5119. [PMID: 376505]
5.  Zhao, X. and Horne, D.A. The role of cysteine residues in the rearrangement of uridine to pseudouridine catalyzed by pseudouridine synthase I. J. Biol. Chem. 272 (1997) 1950–1955. [DOI] [PMID: 8999885]
6.  Foster, P.G., Huang, L., Santi, D.V. and Stroud, R.M. The structural basis for tRNA recognition and pseudouridine formation by pseudouridine synthase I. Nat. Struct. Biol. 7 (2000) 23–27. [DOI] [PMID: 10625422]
7.  Dong, X., Bessho, Y., Shibata, R., Nishimoto, M., Shirouzu, M., Kuramitsu, S. and Yokoyama, S. Crystal structure of tRNA pseudouridine synthase TruA from Thermus thermophilus HB8. RNA Biol. 3 (2006) 115–122. [PMID: 17114947]
8.  Arena, F., Ciliberto, G., Ciampi, S. and Cortese, R. Purification of pseudouridylate synthetase I from Salmonella typhimurium. Nucleic Acids Res. 5 (1978) 4523–4536. [DOI] [PMID: 370771]
[EC 5.4.99.12 created 1990, modified 2011]
 
 
EC 5.4.99.13     
Accepted name: isobutyryl-CoA mutase
Reaction: 2-methylpropanoyl-CoA = butanoyl-CoA
Glossary: pivalate = 2,2-dimethylpropanoate
Other name(s): isobutyryl coenzyme A mutase; butyryl-CoA:isobutyryl-CoA mutase; icmA (gene name); icmB (gene name); icmF (gene name)
Systematic name: 2-methylpropanoyl-CoA CoA-carbonylmutase
Comments: This bacterial enzyme utilizes 5′-deoxyadenosylcobalamin as a cofactor. Following substrate binding, the enzyme catalyses the homolytic cleavage of the cobalt-carbon bond of AdoCbl, yielding cob(II)alamin and a 5′-deoxyadenosyl radical, which initiates the the carbon skeleton rearrangement reaction by hydrogen atom abstraction from the substrate. At the end of each catalytic cycle the 5′-deoxyadenosyl radical and cob(II)alamin recombine, regenerating the resting form of the cofactor. The enzyme is prone to inactivation resulting from occassional loss of the 5′-deoxyadenosyl molecule. Inactivated enzymes are repaired by the action of EC 2.5.1.17, cob(I)yrinic acid a,c-diamide adenosyltransferase, and a G-protein chaperone, which restore cob(II)alamin (which is first reduced to cob(I)alamin by an unidentified reductase) to 5′-deoxyadenosylcobalamin and load it back on the mutase. Some mutases are fused with their G-protein chaperone. These enzyme can also catalyse the interconversion of isovaleryl-CoA with pivalyl-CoA.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 116405-23-3
References:
1.  Brendelberger, G., Rétey, J., Ashworth, D.M., Reynolds, K., Willenbrock, F. and Robinson, J.A. The enzymic interconversion of isobutyryl and N-butyrylcarba(dethia)-coenzyme-A - a coenzyme-B12-dependent carbon skeleton rearrangement. Angew. Chem. Int. Ed. Engl. 27 (1988) 1089–1091.
2.  Ratnatilleke, A., Vrijbloed, J.W. and Robinson, J.A. Cloning and sequencing of the coenzyme B12-binding domain of isobutyryl-CoA mutase from Streptomyces cinnamonensis, reconstitution of mutase activity, and characterization of the recombinant enzyme produced in Escherichia coli. J. Biol. Chem. 274 (1999) 31679–31685. [DOI] [PMID: 10531377]
3.  Cracan, V., Padovani, D. and Banerjee, R. IcmF is a fusion between the radical B12 enzyme isobutyryl-CoA mutase and its G-protein chaperone. J. Biol. Chem. 285 (2010) 655–666. [DOI] [PMID: 19864421]
4.  Cracan, V. and Banerjee, R. Novel coenzyme B12-dependent interconversion of isovaleryl-CoA and pivalyl-CoA. J. Biol. Chem. 287 (2012) 3723–3732. [DOI] [PMID: 22167181]
5.  Jost, M., Born, D.A., Cracan, V., Banerjee, R. and Drennan, C.L. Structural basis for substrate specificity in adenosylcobalamin-dependent isobutyryl-CoA mutase and related acyl-CoA mutases. J. Biol. Chem. 290 (2015) 26882–26898. [DOI] [PMID: 26318610]
6.  Li, Z., Kitanishi, K., Twahir, U.T., Cracan, V., Chapman, D., Warncke, K. and Banerjee, R. Cofactor editing by the G-protein metallochaperone domain regulates the radical B12 enzyme IcmF. J. Biol. Chem. 292 (2017) 3977–3987. [DOI] [PMID: 28130442]
[EC 5.4.99.13 created 1992, revised 2017]
 
 
EC 5.4.99.14     
Accepted name: 4-carboxymethyl-4-methylbutenolide mutase
Reaction: 4-carboxymethyl-4-methylbut-2-en-1,4-olide = 4-carboxymethyl-3-methylbut-2-en-1,4-olide
Other name(s): 4-methyl-2-enelactone isomerase; 4-methylmuconolactone methylisomerase; 4-methyl-3-enelactone methyl isomerase
Systematic name: 4-carboxymethyl-4-methylbut-2-en-1,4-olide methylmutase
Links to other databases: BRENDA, EAWAG-BBD, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 115300-03-3
References:
1.  Bruce, N.C. and Cain, R.B. β-Methylmuconolactone, a key intermediate in the dissimilation of methylaromatic compounds by a modified 3-oxoadipate pathway evolved in nocardioform actinomycetes. FEMS Microbiol. Lett. 50 (1988) 233–239.
[EC 5.4.99.14 created 1992]
 
 


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