BRENDA - Enzyme Database
show all sequences of 4.1.3.24

Enzymic cleavage of malyl-coenzyme A into acetyl-coenzyme A and glyoxylic acid

Tuboi, S.; Kikuchi, G.; Biochim. Biophys. Acta 96, 148-153 (1965)

Data extracted from this reference:

Inhibitors
Inhibitors
Commentary
Organism
Structure
acetyl-CoA
-
Rhodobacter sphaeroides
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.08
-
(3S)-3-carboxy-3-hydroxypropanoyl-CoA
-
Rhodobacter sphaeroides
Metals/Ions
Metals/Ions
Commentary
Organism
Structure
Mg2+
required
Rhodobacter sphaeroides
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Rhodobacter sphaeroides
-
-
-
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
(3S)-3-carboxy-3-hydroxypropanoyl-CoA
-
33259
Rhodobacter sphaeroides
acetyl-CoA + glyoxylate
-
33259
Rhodobacter sphaeroides
?
Inhibitors (protein specific)
Inhibitors
Commentary
Organism
Structure
acetyl-CoA
-
Rhodobacter sphaeroides
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.08
-
(3S)-3-carboxy-3-hydroxypropanoyl-CoA
-
Rhodobacter sphaeroides
Metals/Ions (protein specific)
Metals/Ions
Commentary
Organism
Structure
Mg2+
required
Rhodobacter sphaeroides
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
(3S)-3-carboxy-3-hydroxypropanoyl-CoA
-
33259
Rhodobacter sphaeroides
acetyl-CoA + glyoxylate
-
33259
Rhodobacter sphaeroides
?
Other publictions for EC 4.1.3.24
No.
1st author
Pub Med
title
organims
journal
volume
pages
year
Activating Compound
Application
Cloned(Commentary)
Crystallization (Commentary)
Engineering
General Stability
Inhibitors
KM Value [mM]
Localization
Metals/Ions
Molecular Weight [Da]
Natural Substrates/ Products (Substrates)
Organic Solvent Stability
Organism
Oxidation Stability
Posttranslational Modification
Purification (Commentary)
Reaction
Renatured (Commentary)
Source Tissue
Specific Activity [micromol/min/mg]
Storage Stability
Substrates and Products (Substrate)
Subunits
Temperature Optimum [°C]
Temperature Range [°C]
Temperature Stability [°C]
Turnover Number [1/s]
pH Optimum
pH Range
pH Stability
Cofactor
Ki Value [mM]
pI Value
IC50 Value
Activating Compound (protein specific)
Application (protein specific)
Cloned(Commentary) (protein specific)
Cofactor (protein specific)
Crystallization (Commentary) (protein specific)
Engineering (protein specific)
General Stability (protein specific)
IC50 Value (protein specific)
Inhibitors (protein specific)
Ki Value [mM] (protein specific)
KM Value [mM] (protein specific)
Localization (protein specific)
Metals/Ions (protein specific)
Molecular Weight [Da] (protein specific)
Natural Substrates/ Products (Substrates) (protein specific)
Organic Solvent Stability (protein specific)
Oxidation Stability (protein specific)
Posttranslational Modification (protein specific)
Purification (Commentary) (protein specific)
Renatured (Commentary) (protein specific)
Source Tissue (protein specific)
Specific Activity [micromol/min/mg] (protein specific)
Storage Stability (protein specific)
Substrates and Products (Substrate) (protein specific)
Subunits (protein specific)
Temperature Optimum [°C] (protein specific)
Temperature Range [°C] (protein specific)
Temperature Stability [°C] (protein specific)
Turnover Number [1/s] (protein specific)
pH Optimum (protein specific)
pH Range (protein specific)
pH Stability (protein specific)
pI Value (protein specific)
Expression
General Information
General Information (protein specific)
Expression (protein specific)
KCat/KM [mM/s]
KCat/KM [mM/s] (protein specific)
746671
Gonzalez
Structure of Methylobacterium ...
Methylorubrum extorquens
Acta Crystallogr. Sect. F
73
79-85
2017
-
-
1
1
-
-
1
-
-
1
-
3
-
2
-
-
1
-
-
-
-
-
3
1
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
1
-
-
-
1
-
-
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1
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3
-
-
-
1
-
-
-
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3
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
727258
Zarzycki
The crystal structures of the ...
Chloroflexus aurantiacus, Chloroflexus aurantiacus OK-70-fl / DSM 636, Rhodobacter sphaeroides
BMC Struct. Biol.
13
28
2013
-
-
2
2
-
-
2
-
-
2
4
9
-
6
-
-
2
-
-
-
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-
17
2
-
-
-
-
-
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-
-
-
-
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-
2
-
2
-
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-
2
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2
4
9
-
-
-
2
-
-
-
-
17
2
-
-
-
-
-
-
-
-
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8
8
-
-
-
704322
Erb
The apparent malate synthase a ...
Rhodobacter sphaeroides
J. Bacteriol.
192
1249-1258
2010
1
-
1
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5
6
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2
2
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3
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1
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4
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2
1
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4
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2
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1
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4
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2
1
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4
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1
1
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715363
Okubo
Alternative route for glyoxyla ...
Methylorubrum extorquens, Methylorubrum extorquens ATCC 14718 / DSM 1338 / JCM 2805 / NCIMB 9133 / AM1
J. Bacteriol.
192
1813-1823
2010
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18
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2
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2
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-
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1
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1
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-
665383
Meister
L-Malyl-coenzyme A/beta-methyl ...
Rhodobacter capsulatus
J. Bacteriol.
187
1415-1425
2005
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-
-
-
-
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1
4
-
3
2
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8
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1
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2
3
1
2
1
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1
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4
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3
2
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1
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2
3
1
2
1
-
-
-
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651711
Herter
L-Malyl-coenzyme A lyase/beta- ...
Chloroflexus aurantiacus
J. Bacteriol.
184
5999-6006
2002
-
-
1
-
-
-
1
5
-
1
2
1
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4
-
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1
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4
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3
1
1
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1
1
1
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1
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1
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5
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1
2
1
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1
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4
-
3
1
1
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1
1
1
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651687
Herter
Autotrophic CO(2) fixation by ...
Chloroflexus aurantiacus, Chloroflexus aurantiacus OK-70-fl / DSM 636
J. Bacteriol.
183
4305-4316
2001
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-
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1
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1
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2
-
7
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4
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1
1
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1
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1
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2
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4
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1
1
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33268
Arps
Genetics of serine pathway enz ...
Methylorubrum extorquens
J. Bacteriol.
175
3776-3783
1993
-
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1
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6
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1
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1
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1
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33267
Hacking
-
Malyl-CoA lyase from Methyloba ...
Methylorubrum extorquens
Methods Enzymol.
188
379-391
1990
-
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-
-
-
-
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3
-
4
1
1
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1
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1
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-
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1
2
3
-
-
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1
-
-
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-
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-
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3
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4
1
1
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1
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1
2
3
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-
1
-
-
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-
-
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-
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33260
Fulton
Molecular cloning of a malyl c ...
Methylorubrum extorquens
J. Bacteriol.
160
718-723
1984
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1
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-
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3
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1
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1
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1
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33264
Lynch
Characterization of two new fa ...
Methylobacterium hypolimneticum, Methylobacterium methanolicum
Appl. Environ. Microbiol.
40
400-407
1980
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2
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2
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33262
Hacking
Purification and properties of ...
Methylorubrum extorquens, Pseudomonas sp.
Biochem. J.
139
399-405
1974
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5
3
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4
1
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2
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1
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2
2
4
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1
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1
1
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5
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3
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4
1
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1
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2
2
4
-
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1
-
1
1
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-
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33263
Hersh
Malyl coenzyme A lyase. Mechan ...
Pseudomonas sp.
J. Biol. Chem.
249
5208-5212
1974
-
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5
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1
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1
1
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1
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2
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5
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1
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1
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2
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-
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33266
Salem
Lack of malyl-CoA lyase in a m ...
Methylorubrum extorquens
J. Gen. Microbiol.
81
525-527
1974
-
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-
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1
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2
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2
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1
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2
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856
Hersh
Malate adenosine triphosphate ...
Pseudomonas sp.
J. Biol. Chem.
248
7295-7303
1973
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-
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-
3
-
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1
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1
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1
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3
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3
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1
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1
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3
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33265
Salem
Cleavage of malyl-Coenzyme A i ...
Hyphomicrobium sp., Hyphomicrobium sp. X, Methylococcus capsulatus, Methylorubrum extorquens, Methylosinus trichosporium, Pseudomonas methanolica, Pseudomonas sp., Pseudomonas sp. MA, Pseudomonas sp. MS
Biochem. J.
136
89-96
1973
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9
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25
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18
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9
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18
-
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-
33259
Tuboi
Enzymic cleavage of malyl-coen ...
Rhodobacter sphaeroides
Biochim. Biophys. Acta
96
148-153
1965
-
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1
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