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(2R,3S)-2-methylmalyl-CoA
propanoyl-CoA + glyoxylate
(2S)-4-malyl-CoA
acetyl-CoA + glyoxylate
-
-
-
r
(3S)-3-carboxy-3-hydroxypropanoyl-CoA
acetyl-CoA + glyoxylate
(3S)-malyl-CoA
acetyl-CoA + glyoxylate
-
-
-
r
(S)-malyl-CoA
acetyl-CoA + glyoxylate
acetyl-CoA + glyoxylate
(2S)-4-malyl-CoA
-
-
-
r
acetyl-CoA + glyoxylate
(3S)-3-carboxy-3-hydroxypropanoyl-CoA
acetyl-CoA + glyoxylate
L-malyl-CoA
-
-
-
-
r
beta-methylmalyl-CoA
glyoxylate + propionyl-CoA
propionyl-CoA + glyoxylate
(2S)-4-(beta-methyl)-malyl-CoA
-
-
-
r
propionyl-CoA + glyoxylate
erythro-beta-methylmalyl-CoA
additional information
?
-
(2R,3S)-2-methylmalyl-CoA
propanoyl-CoA + glyoxylate
-
-
-
r
(2R,3S)-2-methylmalyl-CoA
propanoyl-CoA + glyoxylate
the synthesis direction is preferred
-
-
r
(2R,3S)-2-methylmalyl-CoA
propanoyl-CoA + glyoxylate
-
-
-
r
(2R,3S)-2-methylmalyl-CoA
propanoyl-CoA + glyoxylate
the synthesis direction is preferred
-
-
r
(2R,3S)-2-methylmalyl-CoA
propanoyl-CoA + glyoxylate
-
-
-
r
(2R,3S)-2-methylmalyl-CoA
propanoyl-CoA + glyoxylate
the synthesis direction is preferred
-
-
r
(3S)-3-carboxy-3-hydroxypropanoyl-CoA
acetyl-CoA + glyoxylate
-
-
-
?
(3S)-3-carboxy-3-hydroxypropanoyl-CoA
acetyl-CoA + glyoxylate
-
-
-
?
(3S)-3-carboxy-3-hydroxypropanoyl-CoA
acetyl-CoA + glyoxylate
-
-
-
r
(3S)-3-carboxy-3-hydroxypropanoyl-CoA
acetyl-CoA + glyoxylate
-
malyl-CoA
-
r
(3S)-3-carboxy-3-hydroxypropanoyl-CoA
acetyl-CoA + glyoxylate
-
enzyme in 3-hydroxypropionate cycle
-
?
(3S)-3-carboxy-3-hydroxypropanoyl-CoA
acetyl-CoA + glyoxylate
-
-
-
?
(3S)-3-carboxy-3-hydroxypropanoyl-CoA
acetyl-CoA + glyoxylate
-
enzyme in 3-hydroxypropionate cycle
-
?
(3S)-3-carboxy-3-hydroxypropanoyl-CoA
acetyl-CoA + glyoxylate
-
-
-
?
(3S)-3-carboxy-3-hydroxypropanoyl-CoA
acetyl-CoA + glyoxylate
-
-
-
?
(3S)-3-carboxy-3-hydroxypropanoyl-CoA
acetyl-CoA + glyoxylate
Methylobacterium hypolimneticum
-
-
-
?
(3S)-3-carboxy-3-hydroxypropanoyl-CoA
acetyl-CoA + glyoxylate
Methylobacterium methanolicum
-
-
-
?
(3S)-3-carboxy-3-hydroxypropanoyl-CoA
acetyl-CoA + glyoxylate
-
-
-
?
(3S)-3-carboxy-3-hydroxypropanoyl-CoA
acetyl-CoA + glyoxylate
-
-
-
?
(3S)-3-carboxy-3-hydroxypropanoyl-CoA
acetyl-CoA + glyoxylate
-
-
-
?
(3S)-3-carboxy-3-hydroxypropanoyl-CoA
acetyl-CoA + glyoxylate
-
-
-
?
(3S)-3-carboxy-3-hydroxypropanoyl-CoA
acetyl-CoA + glyoxylate
-
-
-
?
(3S)-3-carboxy-3-hydroxypropanoyl-CoA
acetyl-CoA + glyoxylate
-
-
-
r
(3S)-3-carboxy-3-hydroxypropanoyl-CoA
acetyl-CoA + glyoxylate
-
-
-
r
(3S)-3-carboxy-3-hydroxypropanoyl-CoA
acetyl-CoA + glyoxylate
-
-
-
?
(3S)-3-carboxy-3-hydroxypropanoyl-CoA
acetyl-CoA + glyoxylate
Pseudomonas methanolica
-
-
-
?
(3S)-3-carboxy-3-hydroxypropanoyl-CoA
acetyl-CoA + glyoxylate
-
-
-
?
(3S)-3-carboxy-3-hydroxypropanoyl-CoA
acetyl-CoA + glyoxylate
-
-
-
r
(3S)-3-carboxy-3-hydroxypropanoyl-CoA
acetyl-CoA + glyoxylate
-
-
-
r
(3S)-3-carboxy-3-hydroxypropanoyl-CoA
acetyl-CoA + glyoxylate
-
-
-
r
(3S)-3-carboxy-3-hydroxypropanoyl-CoA
acetyl-CoA + glyoxylate
-
-
-
r
(3S)-3-carboxy-3-hydroxypropanoyl-CoA
acetyl-CoA + glyoxylate
-
-
-
?
(3S)-3-carboxy-3-hydroxypropanoyl-CoA
acetyl-CoA + glyoxylate
-
-
-
?
(S)-malyl-CoA
acetyl-CoA + glyoxylate
-
-
-
r
(S)-malyl-CoA
acetyl-CoA + glyoxylate
the cleavage direction is preferred
-
-
r
(S)-malyl-CoA
acetyl-CoA + glyoxylate
-
-
-
r
(S)-malyl-CoA
acetyl-CoA + glyoxylate
the cleavage direction is preferred
-
-
r
(S)-malyl-CoA
acetyl-CoA + glyoxylate
-
-
-
r
acetyl-CoA + glyoxylate
(3S)-3-carboxy-3-hydroxypropanoyl-CoA
-
-
-
r
acetyl-CoA + glyoxylate
(3S)-3-carboxy-3-hydroxypropanoyl-CoA
-
-
-
r
acetyl-CoA + glyoxylate
(3S)-3-carboxy-3-hydroxypropanoyl-CoA
-
-
-
r
acetyl-CoA + glyoxylate
(3S)-3-carboxy-3-hydroxypropanoyl-CoA
-
-
-
r
acetyl-CoA + glyoxylate
(3S)-3-carboxy-3-hydroxypropanoyl-CoA
-
-
-
r
beta-methylmalyl-CoA
glyoxylate + propionyl-CoA
-
-
-
r
beta-methylmalyl-CoA
glyoxylate + propionyl-CoA
-
-
-
-
?
beta-methylmalyl-CoA
glyoxylate + propionyl-CoA
-
-
-
-
?
propionyl-CoA + glyoxylate
erythro-beta-methylmalyl-CoA
-
-
-
?
propionyl-CoA + glyoxylate
erythro-beta-methylmalyl-CoA
-
-
-
-
r
additional information
?
-
malyl-CoA lyase is a promiscuous carbon-carbon bond lyase that catalyzes the reversible cleavage of structurally related CoA thioesters
-
-
?
additional information
?
-
-
malyl-CoA lyase is a promiscuous carbon-carbon bond lyase that catalyzes the reversible cleavage of structurally related CoA thioesters
-
-
?
additional information
?
-
modeling of binding structures of glyoxylate, acetyl-CoA, pyruvate, and Mg2+, overview
-
-
?
additional information
?
-
-
modeling of binding structures of glyoxylate, acetyl-CoA, pyruvate, and Mg2+, overview
-
-
?
additional information
?
-
the enzyme also catalzes the reversible cleavage of (S)-citramalyl-CoA to acetyl-CoA and pyruvate, reaction of EC 4.1.3.25. Malyl-CoA lyase is a promiscuous carbon-carbon bond lyase that catalyzes the reversible cleavage of structurally related CoA thioesters
-
-
?
additional information
?
-
-
the enzyme also catalzes the reversible cleavage of (S)-citramalyl-CoA to acetyl-CoA and pyruvate, reaction of EC 4.1.3.25. Malyl-CoA lyase is a promiscuous carbon-carbon bond lyase that catalyzes the reversible cleavage of structurally related CoA thioesters
-
-
?
additional information
?
-
the enzyme also catalzes the reversible cleavage of (S)-citramalyl-CoA to acetyl-CoA and pyruvate, reaction of EC 4.1.3.25
-
-
?
additional information
?
-
-
the enzyme also catalzes the reversible cleavage of (S)-citramalyl-CoA to acetyl-CoA and pyruvate, reaction of EC 4.1.3.25
-
-
?
additional information
?
-
the enzyme also catalzes the reversible cleavage of (S)-citramalyl-CoA to acetyl-CoA and pyruvate, reaction of EC 4.1.3.25. Malyl-CoA lyase is a promiscuous carbon-carbon bond lyase that catalyzes the reversible cleavage of structurally related CoA thioesters
-
-
?
additional information
?
-
the enzyme also catalzes the reversible cleavage of (S)-citramalyl-CoA to acetyl-CoA and pyruvate, reaction of EC 4.1.3.25
-
-
?
additional information
?
-
-
the role in C1 metabolism, in organisms utilizing the Ser pathway, may be to provide the glyoxylate necessary to sustain operations of this pathway
-
-
?
additional information
?
-
-
the role in C1 metabolism, in organisms utilizing the Ser pathway, may be to provide the glyoxylate necessary to sustain operations of this pathway
-
-
?
additional information
?
-
-
the enzyme may serve as a route to Gly during biosynthesis of purines and proteins
-
-
?
additional information
?
-
-
-
-
-
?
additional information
?
-
-
-
-
-
?
additional information
?
-
-
the role in C1 metabolism, in organisms utilizing the Ser pathway, may be to provide the glyoxylate necessary to sustain operations of this pathway
-
-
?
additional information
?
-
-
the role in C1 metabolism, in organisms utilizing the Ser pathway, may be to provide the glyoxylate necessary to sustain operations of this pathway
-
-
?
additional information
?
-
Pseudomonas methanolica
-
the enzyme may serve as a route to Gly during biosynthesis of purines and proteins
-
-
?
additional information
?
-
-
the specific activity of malyl-CoA lyase is severalfold higher when grown on C1 compounds than when grown on C2, C3 or C4 compounds
-
-
?
additional information
?
-
-
the specific activity of malyl-CoA lyase is severalfold higher when grown on C1 compounds than when grown on C2, C3 or C4 compounds
-
-
?
additional information
?
-
-
the specific activity of malyl-CoA lyase is severalfold higher when grown on C1 compounds than when grown on C2, C3 or C4 compounds
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
(2R,3S)-2-methylmalyl-CoA
propanoyl-CoA + glyoxylate
(2S)-4-malyl-CoA
acetyl-CoA + glyoxylate
-
-
-
r
(3S)-3-carboxy-3-hydroxypropanoyl-CoA
acetyl-CoA + glyoxylate
(S)-malyl-CoA
acetyl-CoA + glyoxylate
acetyl-CoA + glyoxylate
(2S)-4-malyl-CoA
-
-
-
r
propionyl-CoA + glyoxylate
(2S)-4-(beta-methyl)-malyl-CoA
-
-
-
r
additional information
?
-
(2R,3S)-2-methylmalyl-CoA
propanoyl-CoA + glyoxylate
-
-
-
r
(2R,3S)-2-methylmalyl-CoA
propanoyl-CoA + glyoxylate
-
-
-
r
(2R,3S)-2-methylmalyl-CoA
propanoyl-CoA + glyoxylate
-
-
-
r
(3S)-3-carboxy-3-hydroxypropanoyl-CoA
acetyl-CoA + glyoxylate
-
-
-
r
(3S)-3-carboxy-3-hydroxypropanoyl-CoA
acetyl-CoA + glyoxylate
-
enzyme in 3-hydroxypropionate cycle
-
?
(3S)-3-carboxy-3-hydroxypropanoyl-CoA
acetyl-CoA + glyoxylate
-
enzyme in 3-hydroxypropionate cycle
-
?
(S)-malyl-CoA
acetyl-CoA + glyoxylate
-
-
-
r
(S)-malyl-CoA
acetyl-CoA + glyoxylate
-
-
-
r
(S)-malyl-CoA
acetyl-CoA + glyoxylate
-
-
-
r
additional information
?
-
malyl-CoA lyase is a promiscuous carbon-carbon bond lyase that catalyzes the reversible cleavage of structurally related CoA thioesters
-
-
?
additional information
?
-
-
malyl-CoA lyase is a promiscuous carbon-carbon bond lyase that catalyzes the reversible cleavage of structurally related CoA thioesters
-
-
?
additional information
?
-
the enzyme also catalzes the reversible cleavage of (S)-citramalyl-CoA to acetyl-CoA and pyruvate, reaction of EC 4.1.3.25. Malyl-CoA lyase is a promiscuous carbon-carbon bond lyase that catalyzes the reversible cleavage of structurally related CoA thioesters
-
-
?
additional information
?
-
-
the enzyme also catalzes the reversible cleavage of (S)-citramalyl-CoA to acetyl-CoA and pyruvate, reaction of EC 4.1.3.25. Malyl-CoA lyase is a promiscuous carbon-carbon bond lyase that catalyzes the reversible cleavage of structurally related CoA thioesters
-
-
?
additional information
?
-
the enzyme also catalzes the reversible cleavage of (S)-citramalyl-CoA to acetyl-CoA and pyruvate, reaction of EC 4.1.3.25. Malyl-CoA lyase is a promiscuous carbon-carbon bond lyase that catalyzes the reversible cleavage of structurally related CoA thioesters
-
-
?
additional information
?
-
-
the role in C1 metabolism, in organisms utilizing the Ser pathway, may be to provide the glyoxylate necessary to sustain operations of this pathway
-
-
?
additional information
?
-
-
the role in C1 metabolism, in organisms utilizing the Ser pathway, may be to provide the glyoxylate necessary to sustain operations of this pathway
-
-
?
additional information
?
-
-
the enzyme may serve as a route to Gly during biosynthesis of purines and proteins
-
-
?
additional information
?
-
-
-
-
-
?
additional information
?
-
-
-
-
-
?
additional information
?
-
-
the role in C1 metabolism, in organisms utilizing the Ser pathway, may be to provide the glyoxylate necessary to sustain operations of this pathway
-
-
?
additional information
?
-
-
the role in C1 metabolism, in organisms utilizing the Ser pathway, may be to provide the glyoxylate necessary to sustain operations of this pathway
-
-
?
additional information
?
-
Pseudomonas methanolica
-
the enzyme may serve as a route to Gly during biosynthesis of purines and proteins
-
-
?
additional information
?
-
-
the specific activity of malyl-CoA lyase is severalfold higher when grown on C1 compounds than when grown on C2, C3 or C4 compounds
-
-
?
additional information
?
-
-
the specific activity of malyl-CoA lyase is severalfold higher when grown on C1 compounds than when grown on C2, C3 or C4 compounds
-
-
?
additional information
?
-
-
the specific activity of malyl-CoA lyase is severalfold higher when grown on C1 compounds than when grown on C2, C3 or C4 compounds
-
-
?
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evolution
the enzyme belongs to the large superfamily of CitE-like enzymes, which includes the beta-subunit of citrate lyase (CitE), malyl-CoA thioesterases and other enzymes of unknown physiological function. The CitE-like enzyme superfamily also bears sequence and structural resemblance to the malate synthases. All of these different enzymes share highly conserved catalytic residues, although they catalyze distinctly different reactions: C-C bond formation and cleavage, thioester hydrolysis, or both (the malate synthases)
evolution
the enzyme belongs to the large superfamily of CitE-like enzymes, which includes the beta-subunit of citrate lyase (CitE), malyl-CoA thioesterases and other enzymes of unknown physiological function. The CitE-like enzyme superfamily also bears sequence and structural resemblance to the malate synthases. All of these different enzymes share highly conserved catalytic residues, although they catalyze distinctly different reactions: C-C bond formation and cleavage, thioester hydrolysis, or both (the malate synthases)
evolution
-
the enzyme belongs to the large superfamily of CitE-like enzymes, which includes the beta-subunit of citrate lyase (CitE), malyl-CoA thioesterases and other enzymes of unknown physiological function. The CitE-like enzyme superfamily also bears sequence and structural resemblance to the malate synthases. All of these different enzymes share highly conserved catalytic residues, although they catalyze distinctly different reactions: C-C bond formation and cleavage, thioester hydrolysis, or both (the malate synthases)
-
metabolism
Mcl1 and Mcl2 together catalyze the apparent malate synthase activity during acetyl-CoA assimilation via the ethylmalonyl-CoA pathway. Mcl1 is a true (3S)-malyl-CoA lyase, catalyzing the Claisen condensation of acetyl-CoA with glyoxylate. Activity of the mcl1::kan mutant is not detected in cell extracts grown on succinate plus acetate. Apparent malate synthase activity is very low in cell extracts of the mcl1::kan and mcl2::kan mutants when grown on acetate or acetate plus succinate
metabolism
the enzyme belongs to a group of organisms that lack isocitrate lyase. Therefore, they are unable to use the glyoxylate bypass to assimilate acetyl-CoA or other substrates that enter central carbon metabolism at the level of acetyl-CoA. Instead, they use the ethylmalonyl-CoA pathway for the assimilation of acetyl-CoA with the bifunctional enzyme catalyzing the cleavage of beta-methylmalyl-CoA and the synthesis of malyl-CoA
metabolism
the enzyme catalyzes three different steps in the 3-hydroxypropionate bi-cycle for autotrophic CO2 fixation, the tri-functionality of the MCLC underscores its key role for this pathway
metabolism
-
the enzyme catalyzes three different steps in the 3-hydroxypropionate bi-cycle for autotrophic CO2 fixation, the tri-functionality of the MCLC underscores its key role for this pathway
-
physiological function
the enzyme from Rhodobacter sphaeroides is involved in the ethylmalonyl-CoA pathway for acetate assimilation
physiological function
the enzyme plays a crucial, multifunctional role in the 3-hydroxypropionate bi-cycle for autotrophic CO2 fixation in Chloroflexus aurantiacus
physiological function
-
the enzyme plays a crucial, multifunctional role in the 3-hydroxypropionate bi-cycle for autotrophic CO2 fixation in Chloroflexus aurantiacus
-
additional information
upon ligand binding, changes in the C-terminal domains of the enzyme results in closing of the active site, with the C-terminal domain of one monomer forming a lid over and contributing side chains to the active site of the adjacent monomer, overview
additional information
-
upon ligand binding, changes in the C-terminal domains of the enzyme results in closing of the active site, with the C-terminal domain of one monomer forming a lid over and contributing side chains to the active site of the adjacent monomer, overview
additional information
upon ligand binding, changes in the C-terminal domains of the enzyme results in closing of the active site, with the C-terminal domain of one monomer forming a lid over and contributing side chains to the active site of the adjacent monomer, overview
additional information
-
upon ligand binding, changes in the C-terminal domains of the enzyme results in closing of the active site, with the C-terminal domain of one monomer forming a lid over and contributing side chains to the active site of the adjacent monomer, overview
additional information
-
upon ligand binding, changes in the C-terminal domains of the enzyme results in closing of the active site, with the C-terminal domain of one monomer forming a lid over and contributing side chains to the active site of the adjacent monomer, overview
-
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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.
brenda
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
brenda
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
brenda
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.
brenda
Hersh, L.B.
Malyl coenzyme A lyase. Mechanism of action as deduced by kinetic analysis
J. Biol. Chem.
249
5208-5212
1974
Pseudomonas sp.
brenda
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
brenda
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
brenda
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
brenda
Hacking, A.J.; Quayle, J.R.
Malyl-CoA lyase from Methylobacterium extorquens AM1
Methods Enzymol.
188
379-391
1990
Methylorubrum extorquens
-
brenda
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
brenda
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
brenda
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
brenda
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
brenda
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
brenda
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
brenda
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)
brenda
Gonzalez, J.M.; Marti-Arbona, R.; Chen, J.C.; Unkefer, C.J.
Structure of Methylobacterium extorquens malyl-CoA lyase CoA-substrate binding correlates with domain shift
Acta Crystallogr. Sect. F
73
79-85
2017
Methylorubrum extorquens (C5B113), Methylorubrum extorquens
brenda