The Enzyme Database

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EC 1.1.1.37     
Accepted name: malate dehydrogenase
Reaction: (S)-malate + NAD+ = oxaloacetate + NADH + H+
For diagram of the citric-acid cycle, click here and for diagram of the glyoxylate cycle, click here
Other name(s): malic dehydrogenase; L-malate dehydrogenase; NAD-L-malate dehydrogenase; malic acid dehydrogenase; NAD-dependent malic dehydrogenase; NAD-malate dehydrogenase; NAD-malic dehydrogenase; malate (NAD) dehydrogenase; NAD-dependent malate dehydrogenase; NAD-specific malate dehydrogenase; NAD-linked malate dehydrogenase; MDH (ambiguous); L-malate-NAD+ oxidoreductase
Systematic name: (S)-malate:NAD+ oxidoreductase
Comments: There are several forms of malate dehydrogenases that differ by their use of substrate and cofactors. This NAD+-dependent enzyme forms oxaloacetate and unlike EC 1.1.1.38, malate dehydrogenase (oxaloacetate-decarboxylating), is unable to convert it to pyruvate. Also oxidizes some other 2-hydroxydicarboxylic acids. cf. EC 1.1.1.82, malate dehydrogenase (NADP+); EC 1.1.1.299, malate dehydrogenase [NAD(P)+]; and EC 1.1.5.4, malate dehydrogenase (quinone).
Links to other databases: BRENDA, EXPASY, GTD, KEGG, MetaCyc, PDB, CAS registry number: 9001-64-3
References:
1.  Banaszak, L.J. and Bradshaw, R.A. Malate dehydrogenase. In: Boyer, P.D. (Ed.), The Enzymes, 3rd edn, vol. 11, Academic Press, New York, 1975, pp. 369–396.
2.  Guha, A., Englard, S. and Listowsky, I. Beef heart malic dehydrogenases. VII. Reactivity of sulfhydryl groups and conformation of the supernatant enzyme. J. Biol. Chem. 243 (1968) 609–615. [PMID: 5637713]
3.  McReynolds, M.S. and Kitto, G.B. Purification and properties of Drosophila malate dehydrogenases. Biochim. Biophys. Acta 198 (1970) 165–175. [DOI] [PMID: 4313528]
4.  Wolfe, R.G. and Nielands, J.B. Some molecular and kinetic properties of heart malic dehydrogenase. J. Biol. Chem. 221 (1956) 61–69. [PMID: 13345798]
[EC 1.1.1.37 created 1961]
 
 
EC 1.1.1.38     
Accepted name: malate dehydrogenase (oxaloacetate-decarboxylating)
Reaction: (1) (S)-malate + NAD+ = pyruvate + CO2 + NADH
(2) oxaloacetate = pyruvate + CO2
Other name(s): ’malic’ enzyme (ambiguous); pyruvic-malic carboxylase (ambiguous); NAD+-specific malic enzyme; NAD+-malic enzyme; NAD+-linked malic enzyme
Systematic name: (S)-malate:NAD+ oxidoreductase (oxaloacetate-decarboxylating)
Comments: Unlike EC 1.1.1.39, malate dehydrogenase (decarboxylating), this enzyme can also decarboxylate oxaloacetate. cf. EC 1.1.1.40, malate dehydrogenase (oxaloacetate-decarboxylating) (NADP+).
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9080-52-8
References:
1.  Kaufman, S., Korkes, S. and del Campillo, A. Biosynthesis of dicarboxylic acids by carbon dioxide fixation. V. Further studies of the "malic" enzyme of Lactobacillus arabinosus. J. Biol. Chem. 192 (1951) 301–312. [PMID: 14917678]
2.  Yamaguchi, M. Studies on regulatory functions of malic enzymes. IV. Effects of sulfhydryl group modification on the catalytic function of NAD-linked malic enzyme from Escherichia coli. J. Biochem. 86 (1979) 325–333. [PMID: 225306]
[EC 1.1.1.38 created 1961]
 
 
EC 1.1.1.39     
Accepted name: malate dehydrogenase (decarboxylating)
Reaction: (S)-malate + NAD+ = pyruvate + CO2 + NADH
Other name(s): ’malic’ enzyme (ambiguous); pyruvic-malic carboxylase (ambiguous); NAD-specific malic enzyme (ambiguous); NAD-malic enzyme (ambiguous); malate dehydrogenase (decarboxylating) (ambiguous)
Systematic name: (S)-malate:NAD+ oxidoreductase (decarboxylating)
Comments: There are several forms of malate dehydrogenases that differ in their use of substrates and cofactors. This particular form is found only in the plant kingdom. Unlike EC 1.1.1.38, which catalyses a similar reaction, this enzyme can not bind oxaloacetate, and thus does not decarboxylate exogeneously-added oxaloacetate. cf. EC 1.1.1.37, malate dehydrogenase; EC 1.1.1.38, malate dehydrogenase (oxaloacetate-decarboxylating); and EC 1.1.1.83, D-malate dehydrogenase (decarboxylating).
Links to other databases: BRENDA, EXPASY, GTD, KEGG, MetaCyc, CAS registry number: 9028-46-0
References:
1.  Macrae, A.R. Isolation and properties of a ’malic’ enzyme from cauliflower bud mitochondria. Biochem. J. 122 (1971) 495–501. [PMID: 4399380]
2.  Grover, S.D., Canellas, P.F. and Wedding, R.T. Purification of NAD malic enzyme from potato and investigation of some physical and kinetic properties. Arch. Biochem. Biophys. 209 (1981) 396–407. [PMID: 7294802]
3.  Wedding, R.T. and Black, M.K. Physical and kinetic properties and regulation of the NAD malic enzyme purified from leaves of Crassula argentea. Plant Physiol. 72 (1983) 1021–1028. [PMID: 16663114]
4.  Wedding, R.T. Malic enzymes of higher plants: characteristics, regulation, and physiological function. Plant Physiol. 90 (1989) 367–371. [PMID: 16666776]
[EC 1.1.1.39 created 1961]
 
 
EC 1.1.1.40     
Accepted name: malate dehydrogenase (oxaloacetate-decarboxylating) (NADP+)
Reaction: (1) (S)-malate + NADP+ = pyruvate + CO2 + NADPH
(2) oxaloacetate = pyruvate + CO2
Other name(s): ’malic’ enzyme (ambiguous); pyruvic-malic carboxylase (ambiguous); malate dehydrogenase (decarboxylating, NADP+); NADP+-linked decarboxylating malic enzyme; NADP+-malic enzyme; NADP+-specific malic enzyme; NADP+-specific malate dehydrogenase; malate dehydrogenase (NADP+, decarboxylating); L-malate:NADP+ oxidoreductase
Systematic name: (S)-malate:NADP+ oxidoreductase (oxaloacetate-decarboxylating)
Comments: The enzyme catalyses the oxidative decarboxylation of (S)-malate in the presence of NADP+ and divalent metal ions, and the decarboxylation of oxaloacetate. cf. EC 1.1.1.38, malate dehydrogenase (oxaloacetate-decarboxylating), and EC 1.1.1.39, malate dehydrogenase (decarboxylating).
Links to other databases: BRENDA, EXPASY, GTD, KEGG, MetaCyc, PDB, CAS registry number: 9028-47-1
References:
1.  Harary, I., Korey, S.R. and Ochoa, S. Biosynthesis of dicarboxylic acids by carbon dioxide fixation. VII. Equilibrium of "malic" enzyme reaction. J. Biol. Chem. 203 (1953) 595–604. [PMID: 13084629]
2.  Ochoa, S., Mehler, A.H. and Kornberg, A. Biosynthesis of dicarboxylic acids by carbon dioxide fixation. I. Isolation and properties of an enzyme from pigeon liver catalyzing the reversible oxidative decarboxylation of l-malic acid. J. Biol. Chem. 174 (1948) 979–1000. [PMID: 18871257]
3.  Rutter, W.J. and Lardy, H.A. Purification and properties of pigeon liver malic enzyme. J. Biol. Chem. 233 (1958) 374–382. [PMID: 13563505]
4.  Stickland, R.G. Some properties of the malic enzyme of pigeon liver. 1. Conversion of malate into pyruvate. Biochem. J. 73 (1959) 646–654. [PMID: 13834656]
5.  Stickland, R.G. Some properties of the malic enzyme of pigeon liver. 2. Synthesis of malate from pyruvate. Biochem. J. 73 (1959) 654–659. [PMID: 13834657]
6.  Walker, D.A. Physiological studies on acid metabolism. 7. Malic enzyme from KalanchoĆ« crenata: effects of carbon dioxide concentration. Biochem. J. 74 (1960) 216–223. [PMID: 13842495]
[EC 1.1.1.40 created 1961, modified 1976]
 
 
EC 1.1.1.82     
Accepted name: malate dehydrogenase (NADP+)
Reaction: (S)-malate + NADP+ = oxaloacetate + NADPH + H+
Other name(s): NADP-malic enzyme; NADP-malate dehydrogenase; malic dehydrogenase (nicotinamide adenine dinucleotide phosphate); malate NADP dehydrogenase; NADP malate dehydrogenase; NADP-linked malate dehydrogenase; malate dehydrogenase (NADP)
Systematic name: (S)-malate:NADP+ oxidoreductase
Comments: Activated by light.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 37250-19-4
References:
1.  Connelly, J.L., Danner, D.J. and Bowden, J.A. Branched chain α-keto acid metabolism. I. Isolation, purification, and partial characterization of bovine liver α-ketoisocaproic:α-keto-β-methylvaleric acid dehydrogenase. J. Biol. Chem. 243 (1968) 1198–1203. [PMID: 5689906]
2.  Johnson, H.S. NADP-malate dehydrogenase: photoactivation in leaves of plants with Calvin cycle photosynthesis. Biochem. Biophys. Res. Commun. 43 (1971) 703–709. [DOI] [PMID: 4397919]
3.  Johnson, H.S. and Hatch, M.D. Properties and regulation of leaf nicotinamide-adenine dinucleotide phosphate-malate dehydrogenase and 'malic' enzyme in plants with the C4-dicarboxylic acid pathway of photosynthesis. Biochem. J. 119 (1970) 273–280. [PMID: 4395182]
[EC 1.1.1.82 created 1972]
 
 
EC 1.1.1.299     
Accepted name: malate dehydrogenase [NAD(P)+]
Reaction: (S)-malate + NAD(P)+ = oxaloacetate + NAD(P)H + H+
Other name(s): MdH II, NAD(P)+-dependent malate dehyrogenase
Systematic name: (S)-malate:NAD(P)+ oxidoreductase
Comments: This enzyme, which was characterized from the methanogenic archaeon Methanobacterium thermoautotrophicum, catalyses only the reduction of oxaloacetate, and can use NAD+ and NADP+ with similar specific activity [1]. Different from EC 1.1.1.37 (malate dehydrogenase (NAD+)), EC 1.1.1.82 (malate dehydrogenase (NADP+)) and EC 1.1.5.4 (malate dehydrogenase (quinone)).
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Thompson, H., Tersteegen, A., Thauer, R.K. and Hedderich, R. Two malate dehydrogenases in Methanobacterium thermoautotrophicum. Arch. Microbiol. 170 (1998) 38–42. [PMID: 9639601]
[EC 1.1.1.299 created 2009]
 
 
EC 1.1.1.337     
Accepted name: L-2-hydroxycarboxylate dehydrogenase (NAD+)
Reaction: a (2S)-2-hydroxycarboxylate + NAD+ = a 2-oxocarboxylate + NADH + H+
Other name(s): (R)-sulfolactate:NAD+ oxidoreductase; L-sulfolactate dehydrogenase; (R)-sulfolactate dehydrogenase; L-2-hydroxyacid dehydrogenase (NAD+); ComC
Systematic name: (2S)-2-hydroxycarboxylate:NAD+ oxidoreductase
Comments: The enzyme from the archaeon Methanocaldococcus jannaschii acts on multiple (S)-2-hydroxycarboxylates including (2R)-3-sulfolactate, (S)-malate, (S)-lactate, and (S)-2-hydroxyglutarate [3]. Note that (2R)-3-sulfolactate has the same stereo configuration as (2S)-2-hydroxycarboxylates.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 81210-65-3
References:
1.  Graupner, M., Xu, H. and White, R.H. Identification of an archaeal 2-hydroxy acid dehydrogenase catalyzing reactions involved in coenzyme biosynthesis in methanoarchaea. J. Bacteriol. 182 (2000) 3688–3692. [DOI] [PMID: 10850983]
2.  Graupner, M. and White, R.H. The first examples of (S)-2-hydroxyacid dehydrogenases catalyzing the transfer of the pro-4S hydrogen of NADH are found in the archaea. Biochim. Biophys. Acta 1548 (2001) 169–173. [DOI] [PMID: 11451450]
3.  Graham, D.E. and White, R.H. Elucidation of methanogenic coenzyme biosyntheses: from spectroscopy to genomics. Nat. Prod. Rep. 19 (2002) 133–147. [PMID: 12013276]
4.  Rein, U., Gueta, R., Denger, K., Ruff, J., Hollemeyer, K. and Cook, A.M. Dissimilation of cysteate via 3-sulfolactate sulfo-lyase and a sulfate exporter in Paracoccus pantotrophus NKNCYSA. Microbiology 151 (2005) 737–747. [DOI] [PMID: 15758220]
[EC 1.1.1.337 created 2012]
 
 
EC 1.1.1.338     
Accepted name: (2R)-3-sulfolactate dehydrogenase (NADP+)
Reaction: (2R)-3-sulfolactate + NADP+ = 3-sulfopyruvate + NADPH + H+
For diagram of coenzyme-M biosynthesis, click here
Other name(s): (R)-sulfolactate:NADP+ oxidoreductase; L-sulfolactate dehydrogenase; (R)-sulfolactate dehydrogenase; ComC
Systematic name: (2R)-3-sulfolactate:NADP+ oxidoreductase
Comments: The enzyme from the bacterium Chromohalobacter salexigens can only utilize NADP+. It functions both biosynthetically in coenzyme M biosynthesis and degradatively, in the degradation of sulfolactate. It can not use (S)-malate and (S)-lactate.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 81210-65-3
References:
1.  Denger, K. and Cook, A.M. Racemase activity effected by two dehydrogenases in sulfolactate degradation by Chromohalobacter salexigens: purification of (S)-sulfolactate dehydrogenase. Microbiology 156 (2010) 967–974. [DOI] [PMID: 20007648]
[EC 1.1.1.338 created 2012]
 
 
EC 1.1.1.375     
Accepted name: L-2-hydroxycarboxylate dehydrogenase [NAD(P)+]
Reaction: a (2S)-2-hydroxycarboxylate + NAD(P)+ = a 2-oxocarboxylate + NAD(P)H + H+
Other name(s): MdhII; lactate/malate dehydrogenase
Systematic name: (2S)-2-hydroxycarboxylate:NAD(P)+ oxidoreductase
Comments: The enzyme from the archaeon Methanocaldococcus jannaschii catalyses the reversible oxidation of (2R)-3-sulfolactate and (S)-malate to 3-sulfopyruvate and oxaloacetate, respectively (note that (2R)-3-sulfolactate has the same stereochemical configuration as (2S)-2-hydroxycarboxylates) [1]. The enzyme can use both NADH and NADPH, although activity is higher with NADPH [1-3]. The oxidation of (2R)-3-sulfolactate was observed only in the presence of NADP+ [1]. The same organism also possesses an NAD+-specific enzyme with similar activity, cf. EC 1.1.1.337, L-2-hydroxycarboxylate dehydrogenase (NAD+).
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Graupner, M., Xu, H. and White, R.H. Identification of an archaeal 2-hydroxy acid dehydrogenase catalyzing reactions involved in coenzyme biosynthesis in methanoarchaea. J. Bacteriol. 182 (2000) 3688–3692. [DOI] [PMID: 10850983]
2.  Lee, B.I., Chang, C., Cho, S.J., Eom, S.H., Kim, K.K., Yu, Y.G. and Suh, S.W. Crystal structure of the MJ0490 gene product of the hyperthermophilic archaebacterium Methanococcus jannaschii, a novel member of the lactate/malate family of dehydrogenases. J. Mol. Biol. 307 (2001) 1351–1362. [DOI] [PMID: 11292347]
3.  Madern, D. The putative L-lactate dehydrogenase from Methanococcus jannaschii is an NADPH-dependent L-malate dehydrogenase. Mol. Microbiol. 37 (2000) 1515–1520. [DOI] [PMID: 10998181]
[EC 1.1.1.375 created 2014]
 
 
EC 1.1.3.3      
Deleted entry: malate oxidase. Now classified as EC 1.1.5.4, malate dehydrogenase (quinone).
[EC 1.1.3.3 created 1961, deleted 2014]
 
 
EC 1.1.5.4     
Accepted name: malate dehydrogenase (quinone)
Reaction: (S)-malate + a quinone = oxaloacetate + reduced quinone
Other name(s): FAD-dependent malate-vitamin K reductase; malate-vitamin K reductase; (S)-malate:(acceptor) oxidoreductase; L-malate-quinone oxidoreductase; malate:quinone oxidoreductase; malate quinone oxidoreductase; MQO; malate:quinone reductase; malate dehydrogenase (acceptor); FAD-dependent malate dehydrogenase
Systematic name: (S)-malate:quinone oxidoreductase
Comments: A flavoprotein (FAD). Vitamin K and several other quinones can act as acceptors. Different from EC 1.1.1.37 (malate dehydrogenase (NAD+)), EC 1.1.1.82 (malate dehydrogenase (NADP+)) and EC 1.1.1.299 (malate dehydrogenase [NAD(P)+]).
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Imai, D. and Brodie, A.F. A phospholipid-requiring enzyme, malate-vitamin K reductase. J. Biol. Chem. 248 (1973) 7487–7494.
2.  Imai, T. FAD-dependent malate dehydrogenase, a phospholipid-requiring enzyme from Mycobacterium sp. strain Takeo. Purification and some properties. Biochim. Biophys. Acta 523 (1978) 37–46. [DOI] [PMID: 629992]
3.  Reddy, T.L.P., Suryanarayana, P.M. and Venkitasubramanian, T.A. Variations in the pathways of malate oxidation and phosphorylation in different species of Mycobacteria. Biochim. Biophys. Acta 376 (1975) 210–218. [DOI] [PMID: 234747]
4.  Molenaar, D., van der Rest, M.E. and Petrovic, S. Biochemical and genetic characterization of the membrane-associated malate dehydrogenase (acceptor) from Corynebacterium glutamicum. Eur. J. Biochem. 254 (1998) 395–403. [DOI] [PMID: 9660197]
5.  Kather, B., Stingl, K., van der Rest, M.E., Altendorf, K. and Molenaar, D. Another unusual type of citric acid cycle enzyme in Helicobacter pylori: the malate:quinone oxidoreductase. J. Bacteriol. 182 (2000) 3204–3209. [DOI] [PMID: 10809701]
[EC 1.1.5.4 created 1978 as EC 1.1.99.16, transferred 2009 to EC 1.1.5.4]
 
 
EC 1.1.99.16      
Transferred entry: malate dehydrogenase (acceptor). As the acceptor is now known, the enzyme has been transferred to EC 1.1.5.4, malate dehydrogenase (quinone).
[EC 1.1.99.16 created 1978, deleted 2009]
 
 
EC 2.3.1.92     
Accepted name: sinapoylglucose—malate O-sinapoyltransferase
Reaction: 1-O-sinapoyl-β-D-glucose + (S)-malate = D-glucose + sinapoyl-(S)-malate
Other name(s): 1-sinapoylglucose-L-malate sinapoyltransferase; sinapoylglucose:malate sinapoyltransferase
Systematic name: 1-O-sinapoyl-β-D-glucose:(S)-malate O-sinapoyltransferase
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 76095-65-3
References:
1.  Strack, D. Development of 1-O-sinapoyl-β-D-glucose-l-malate sinapoyltransferase activity in cotyledons of red radish (Raphanus sativus L. var sativus). Planta 155 (1982) 31–36. [PMID: 24271623]
[EC 2.3.1.92 created 1986]
 
 
EC 2.3.3.9     
Accepted name: malate synthase
Reaction: acetyl-CoA + glyoxylate + H2O = (S)-malate + CoA
For diagram of the glyoxylate cycle, click here
Other name(s): L-malate glyoxylate-lyase (CoA-acetylating); glyoxylate transacetylase; glyoxylate transacetase; glyoxylic transacetase; malate condensing enzyme; malate synthetase; malic synthetase; malic-condensing enzyme; acetyl-CoA:glyoxylate C-acetyltransferase (thioester-hydrolysing, carboxymethyl-forming)
Systematic name: acetyl-CoA:glyoxylate C-acetyltransferase [(S)-malate-forming]
Comments: The enzyme catalyses the irreversible condensation of acetyl-CoA with glyoxylate to form (S)-malate. Among other functions, the enzyme participates in the glyoxylate cycle, a modified version of the TCA cycle that bypasses steps that lead to a loss of CO2.
Links to other databases: BRENDA, EXPASY, GTD, KEGG, MetaCyc, PDB, CAS registry number: 9013-48-3
References:
1.  Dixon, G.H., Kornberg, H.L. and Lund, P. Purification and properties of malate synthetase. Biochim. Biophys. Acta 41 (1960) 217–233. [DOI] [PMID: 13816984]
2.  Molina, I., Pellicer, M.T., Badia, J., Aguilar, J. and Baldoma, L. Molecular characterization of Escherichia coli malate synthase G. Differentiation with the malate synthase A isoenzyme. Eur. J. Biochem. 224 (1994) 541–548. [DOI] [PMID: 7925370]
3.  Anstrom, D.M., Kallio, K. and Remington, S.J. Structure of the Escherichia coli malate synthase G:pyruvate:acetyl-coenzyme A abortive ternary complex at 1.95 Å resolution. Protein Sci. 12 (2003) 1822–1832. [DOI] [PMID: 12930982]
4.  Smith, C.V., Huang, C.C., Miczak, A., Russell, D.G., Sacchettini, J.C. and Honer zu Bentrup, K. Biochemical and structural studies of malate synthase from Mycobacterium tuberculosis. J. Biol. Chem. 278 (2003) 1735–1743. [DOI] [PMID: 12393860]
[EC 2.3.3.9 created 1961 as EC 4.1.3.2, transferred 2002 to EC 2.3.3.9]
 
 
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 3.1.2.30     
Accepted name: (3S)-malyl-CoA thioesterase
Reaction: (S)-malyl-CoA + H2O = (S)-malate + CoA
Glossary: (S)-malate = (2S)-2-hydroxybutanedioate
(S)-malyl-CoA = (3S)-3-carboxy-3-hydroxypropanoyl-CoA
Other name(s): mcl2 (gene name)
Systematic name: (S)-malyl-CoA hydrolase
Comments: Stimulated by Mg2+ or Mn2+. The enzyme has no activity with (2R,3S)-2-methylmalyl-CoA (cf. EC 4.1.3.24, malyl-CoA lyase) or other CoA esters.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Erb, T.J., Frerichs-Revermann, L., Fuchs, G. and Alber, B.E. The apparent malate synthase activity of Rhodobacter sphaeroides is due to two paralogous enzymes, (3S)-malyl-coenzyme A (CoA)/β-methylmalyl-CoA lyase and (3S)-malyl-CoA thioesterase. J. Bacteriol. 192 (2010) 1249–1258. [DOI] [PMID: 20047909]
[EC 3.1.2.30 created 2014]
 
 
EC 4.1.1.101     
Accepted name: malolactic enzyme
Reaction: (S)-malate = (S)-lactate + CO2
Other name(s): mleA (gene name); mleS (gene name)
Systematic name: (S)-malate carboxy-lyase
Comments: The enzyme is involved in the malolactic fermentation of wine, which results in a natural decrease in acidity and favorable changes in wine flavors. It has been purified from several lactic acid bacteria, including Leuconostoc mesenteroides [1], Lactobacillus plantarum [2], and Oenococcus oeni [3,4]. The enzyme contains a tightly bound NAD+ cofactor and requires Mn2+.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Lonvaud-Funel, A. and de Saad, A.M. Purification and properties of a malolactic Enzyme from a strain of Leuconostoc mesenteroides isolated from grapes. Appl. Environ. Microbiol. 43 (1982) 357–361. [PMID: 16345941]
2.  Caspritz, G. and Radler, F. Malolactic enzyme of Lactobacillus plantarum. Purification, properties, and distribution among bacteria. J. Biol. Chem. 258 (1983) 4907–4910. [PMID: 6833282]
3.  Naouri, P., Chagnaud, P., Arnaud, A. and Galzy, P. Purification and properties of a malolactic enzyme from Leuconostoc oenos ATCC 23278. J. Basic Microbiol. 30 (1990) 577–585. [DOI] [PMID: 2097345]
4.  Schumann, C., Michlmayr, H., Del Hierro, A.M., Kulbe, K.D., Jiranek, V., Eder, R. and Nguyen, T.H. Malolactic enzyme from Oenococcus oeni: heterologous expression in Escherichia coli and biochemical characterization. Bioengineered 4 (2013) 147–152. [DOI] [PMID: 23196745]
[EC 4.1.1.101 created 2015]
 
 
EC 4.2.1.2     
Accepted name: fumarate hydratase
Reaction: (S)-malate = fumarate + H2O
For diagram of the citric-acid cycle, click here
Other name(s): fumarase; L-malate hydro-lyase; (S)-malate hydro-lyase
Systematic name: (S)-malate hydro-lyase (fumarate-forming)
Links to other databases: BRENDA, EXPASY, GTD, KEGG, MetaCyc, PDB, CAS registry number: 9032-88-6
References:
1.  Alberty, R.A. Fumarase. In: Boyer, P.D., Lardy, H. and Myrbäck, K. (Ed.), The Enzymes, 2nd edn, vol. 5, Academic Press, New York, 1961, pp. 531–544.
2.  Kanarek, L. and Hill, R.L. The preparation and characterization of fumarase from swine heart muscle. J. Biol. Chem. 239 (1964) 4202–4206. [PMID: 14247669]
[EC 4.2.1.2 created 1961]
 
 
EC 4.2.1.34     
Accepted name: (S)-2-methylmalate dehydratase
Reaction: (S)-2-methylmalate = 2-methylfumarate + H2O
Other name(s): mesaconate hydratase; (+)-citramalate hydro-lyase; L-citramalate hydrolase; citramalate dehydratase; (+)-citramalic hydro-lyase; mesaconate mesaconase; mesaconase; (S)-2-methylmalate hydro-lyase
Systematic name: (S)-2-methylmalate hydro-lyase (2-methylfumarate-forming)
Comments: Also hydrates fumarate to (S)-malate.
Links to other databases: BRENDA, EXPASY, GTD, KEGG, MetaCyc, CAS registry number: 9027-94-5
References:
1.  Blair, A.H. and Barker, H.A. Assay and purification of (+)-citramalate hydro-lyase components from Clostridium tetanomorphum. J. Biol. Chem. 241 (1966) 400–408. [PMID: 5903732]
2.  Wang, C.C. and Barker, H.A. Purification and properties of L-citramalate hydrolyase. J. Biol. Chem. 244 (1969) 2516–2526. [PMID: 5769987]
[EC 4.2.1.34 created 1972]
 
 


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