Reference on EC 4.1.3.24 - malyl-CoA lyase
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REF. 
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Hersh, L.B.
Malate adenosine triphosphate lyase. Separation of the reaction into a malate thiokinase and malyl coenzyme A lyase
J. Biol. Chem.
248
7295-7303
1973
Pseudomonas sp.
Tuboi, S.; Kikuchi, G.
Enzymic cleavage of malyl-coenzyme A into acetyl-coenzyme A and glyoxylic acid
Biochim. Biophys. Acta
96
148-153
1965
Cereibacter sphaeroides
Fulton, G.L.; Nunn, D.N.; Lidstrom, M.E.
Molecular cloning of a malyl coenzyme A lyase gene from Pseudomonas sp. strain AM1, a facultative methylotroph
J. Bacteriol.
160
718-723
1984
Methylorubrum extorquens
Hacking, A.J.; Quayle, J.R.
Purification and properties of malyl-coenzyme A lyase from Pseudomonas AM1
Biochem. J.
139
399-405
1974
Methylorubrum extorquens, Pseudomonas sp.
Hersh, L.B.
Malyl coenzyme A lyase. Mechanism of action as deduced by kinetic analysis
J. Biol. Chem.
249
5208-5212
1974
Pseudomonas sp.
Lynch, M.J.; Wopat, A.E.; O'Connor, M.L.
Characterization of two new facultative methanotrophs
Appl. Environ. Microbiol.
40
400-407
1980
Methylobacterium hypolimneticum, Methylobacterium methanolicum
Salem, A.R.; Hacking, A.J.; Quayle, J.R.
Cleavage of malyl-Coenzyme A into acetyl-Coenzyme A and glyoxylate by Pseudomonas AM1 and other C1-unit-utilizing bacteria
Biochem. J.
136
89-96
1973
Hyphomicrobium sp., Methylorubrum extorquens, Methylococcus capsulatus, Methylosinus trichosporium, Pseudomonas sp., Pseudomonas methanolica, Pseudomonas sp. MS, Pseudomonas sp. MA, Hyphomicrobium sp. X
Salem, A.R.; Hacking, A.J.; Quayle, J.R.
Lack of malyl-CoA lyase in a mutant of Pseudomonas AM1
J. Gen. Microbiol.
81
525-527
1974
Methylorubrum extorquens
Hacking, A.J.; Quayle, J.R.
Malyl-CoA lyase from Methylobacterium extorquens AM1
Methods Enzymol.
188
379-391
1990
Methylorubrum extorquens
-
Arps, P.J.; Fulton, G.F.; Minnich, E.C.; Lidstrom, M.E.
Genetics of serine pathway enzymes in Methylobacterium extorquens AM1: phosphoenolpyruvate carboxylase and malyl coenzyme A lyase
J. Bacteriol.
175
3776-3783
1993
Methylorubrum extorquens
Herter, S.; Farfsing, J.; Gad'On, N.; Rieder, C.; Eisenreich, W.; Bacher, A.; Fuchs, G.
Autotrophic CO(2) fixation by Chloroflexus aurantiacus: study of glyoxylate formation and assimilation via the 3-hydroxypropionate cycle
J. Bacteriol.
183
4305-4316
2001
Chloroflexus aurantiacus, Chloroflexus aurantiacus OK-70-fl / DSM 636
Herter, S.; Busch, A.; Fuchs, G.
L-Malyl-coenzyme A lyase/beta-methylmalyl-coenzyme A lyase from Chloroflexus aurantiacus, a bifunctional enzyme involved in autotrophic CO(2) fixation
J. Bacteriol.
184
5999-6006
2002
Chloroflexus aurantiacus
Meister, M.; Saum, S.; Alber, B.E.; Fuchs, G.
L-Malyl-coenzyme A/beta-methylmalyl-coenzyme A lyase is involved in acetate assimilation of the isocitrate lyase-negative bacterium Rhodobacter capsulatus
J. Bacteriol.
187
1415-1425
2005
Rhodobacter capsulatus
Erb, T.J.; Frerichs-Revermann, L.; Fuchs, G.; Alber, B.E.
The apparent malate synthase activity of Rhodobacter sphaeroides is due to two paralogous enzymes, (3S)-Malyl-coenzyme A (CoA)/{beta}-methylmalyl-CoA lyase and (3S)-Malyl-CoA thioesterase
J. Bacteriol.
192
1249-1258
2010
Cereibacter sphaeroides (Q3J5L6), Cereibacter sphaeroides
Okubo, Y.; Yang, S.; Chistoserdova, L.; Lidstrom, M.E.
Alternative route for glyoxylate consumption during growth on two-carbon compounds by Methylobacterium extorquens AM1
J. Bacteriol.
192
1813-1823
2010
Methylorubrum extorquens, Methylorubrum extorquens ATCC 14718 / DSM 1338 / JCM 2805 / NCIMB 9133 / AM1
Zarzycki, J.; Kerfeld, C.A.
The crystal structures of the tri-functional Chloroflexus aurantiacus and bi-functional Rhodobacter sphaeroides malyl-CoA lyases and comparison with CitE-like superfamily enzymes and malate synthases
BMC Struct. Biol.
13
28
2013
Cereibacter sphaeroides (Q3J5L6), Cereibacter sphaeroides, Chloroflexus aurantiacus (S5N020), Chloroflexus aurantiacus, Chloroflexus aurantiacus OK-70-fl / DSM 636 (S5N020)
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