Any feedback?
No. of entries
Information on EC 6.2.1.9 - malate-CoA ligase
for references in articles please use BRENDA:EC6.2.1.9
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree 6 Ligases
6.2 Forming carbon-sulfur bonds
6.2.1 Acid-thiol ligases
6.2.1.9 malate-CoA ligase
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
- 6.2.1.9
- succinyl-coa
- succinate
-
methylobacterium
- phosphoenzyme
- glyoxylate
- methanol
-
extorquens
- carboxylase
-
feedstock
- xylose
-
enzyme-bound
showSynonyms
malate thiokinase, malate-coa ligase, more
topPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
Malate thiokinase
-
-
-
-
Malyl coenzyme A synthetase
-
-
-
-
Malyl-CoA synthetase
-
-
-
-
MTK-alpha
-
-
-
-
MTK-beta
-
-
-
-
Synthetase, malyl coenzyme A
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ATP + malate + CoA = ADP + phosphate + malyl-CoA
random site reaction mechanism
-
ATP + malate + CoA = ADP + phosphate + malyl-CoA
random site reaction mechanism
-
-
ATP + malate + CoA = ADP + phosphate + malyl-CoA
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Acid-thiol ligation
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PATHWAY SOURCE
PATHWAYS
KEGG
MetaCyc
ethylmalonyl-CoA pathway, formaldehyde assimilation I (serine pathway)
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SYSTEMATIC NAME
IUBMB Comments
malate:CoA ligase (ADP-forming)
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CAS REGISTRY NUMBER
COMMENTARY
37318-58-4
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
ATP + 2-mercaptosuccinate + CoA
ADP + phosphate + 2-mercaptosuccinyl-CoA
-
Substrates: activity is 18% relative to L-malate
Products: -
Products: -
?
ATP + butyrate + CoA
ADP + phosphate + butyryl-CoA
-
Substrates: -
Products: -
Products: -
?
ATP + butyrate + CoA
ADP + phosphate + butyryl-CoA
Aureobasidium pullulans CCTCC M2012223
-
Substrates: -
Products: -
Products: -
?
ATP + DL-isocitrate + CoA
ADP + phosphate + isocitryl-CoA
-
Substrates: activity is 27% of the activity relative to L-malate
Products: -
Products: -
?
ATP + DL-isocitrate + CoA
ADP + phosphate + isocitryl-CoA
-
Substrates: activity is 27% of the activity relative to L-malate
Products: -
Products: -
?
ATP + malate + CoA
?
Methanogenic bacterium
-
Substrates: malate:CoA ligase is involved in glycolate degradation pathway under strict anaerobic conditions
Products: -
Products: -
?
ATP + malate + CoA
ADP + phosphate + malyl-CoA
-
Substrates: -
Products: -
Products: -
?
ATP + malate + CoA
ADP + phosphate + malyl-CoA
Aureobasidium pullulans CCTCC M2012223
-
Substrates: -
Products: -
Products: -
?
ATP + malate + CoA
ADP + phosphate + malyl-CoA
Methanogenic bacterium
-
Substrates: -
Products: -
Products: -
?
ATP + malate + CoA
ADP + phosphate + malyl-CoA
-
Substrates: -
Products: -
Products: -
?
ATP + malate + CoA
ADP + phosphate + malyl-CoA
-
Substrates: activity with D-malate is 28% relative to L-malate
Products: -
Products: -
?
ATP + malate + CoA
ADP + phosphate + malyl-CoA
-
Substrates: -
Products: -
Products: -
?
ATP + malate + CoA
ADP + phosphate + malyl-CoA
-
Substrates: -
Products: -
Products: -
?
ATP + malate + CoA
ADP + phosphate + malyl-CoA
-
Substrates: activity with D-malate is 28% relative to L-malate
Products: -
Products: -
?
ATP + malonate + CoA
ADP + phosphate + malonyl-CoA
-
Substrates: -
Products: -
Products: -
?
ATP + malonate + CoA
ADP + phosphate + malonyl-CoA
Aureobasidium pullulans CCTCC M2012223
-
Substrates: -
Products: -
Products: -
?
ATP + oxalate + CoA
ADP + phosphate + oxalyl-CoA
-
Substrates: -
Products: -
Products: -
?
ATP + oxalate + CoA
ADP + phosphate + oxalyl-CoA
Aureobasidium pullulans CCTCC M2012223
-
Substrates: -
Products: -
Products: -
?
ATP + oxaloacetate + CoA
ADP + phosphate + oxaloacetyl-CoA
-
Substrates: -
Products: -
Products: -
?
ATP + oxaloacetate + CoA
ADP + phosphate + oxaloacetyl-CoA
Aureobasidium pullulans CCTCC M2012223
-
Substrates: -
Products: -
Products: -
?
ATP + succinate + CoA
ADP + phosphate + succinyl-CoA
-
Substrates: r
Products: -
Products: -
?
ATP + succinate + CoA
ADP + phosphate + succinyl-CoA
-
Substrates: activity is 105% relative to L-malate
Products: -
Products: -
?
ATP + succinate + CoA
ADP + phosphate + succinyl-CoA
-
Substrates: random addition of substrates
Products: -
Products: -
?
ATP + succinate + CoA
ADP + phosphate + succinyl-CoA
-
Substrates: r
Products: -
Products: -
?
ATP + succinate + CoA
ADP + phosphate + succinyl-CoA
-
Substrates: random addition of substrates
Products: -
Products: -
?
ATP + succinate + CoA
ADP + phosphate + succinyl-CoA
-
Substrates: activity is 105% relative to L-malate
Products: -
Products: -
?
additional information
?
-
-
Substrates: arsenoslysis reaction is sequentially ordered, with succinyl-CoA binding prior to arsenate
Products: -
Products: -
?
additional information
?
-
-
Substrates: enzyme catalyzes a slow ATP-ADP exchange reaction which is stimulated by coenzyme A or succinyl-CoA, and a slow succinate-succinyl-CoA exchange reaction, which requires phosphate
Products: -
Products: -
?
additional information
?
-
-
Substrates: arsenoslysis reaction is sequentially ordered, with succinyl-CoA binding prior to arsenate
Products: -
Products: -
?
additional information
?
-
-
Substrates: enzyme catalyzes a slow ATP-ADP exchange reaction which is stimulated by coenzyme A or succinyl-CoA, and a slow succinate-succinyl-CoA exchange reaction, which requires phosphate
Products: -
Products: -
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
ATP + malate + CoA
?
Methanogenic bacterium
-
Substrates: malate:CoA ligase is involved in glycolate degradation pathway under strict anaerobic conditions
Products: -
Products: -
?
ATP + malate + CoA
ADP + phosphate + malyl-CoA
-
Substrates: -
Products: -
Products: -
?
ATP + malate + CoA
ADP + phosphate + malyl-CoA
Aureobasidium pullulans CCTCC M2012223
-
Substrates: -
Products: -
Products: -
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
ATP
-
high substrate concentrations of ATP inhibit the enzyme activity
Methoxycarbonyl-CoA disulfide
-
ATP protects, low concentrations of succinyl-CoA protect, L-malate protects only in absence of added sulfate. The inhibitor produces half-of-the-sites reactivity with respect to enzyme phosphorylation
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Methanogenic bacterium
coculture of Methanospirillum hungatii strain SK, Acetobacterium woodii, and Desulfovibrio vulgaris strain Marburg
-
-
brenda
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). MTKA_METEA
Methylorubrum extorquens (strain ATCC 14718 / DSM 1338 / JCM 2805 / NCIMB 9133 / AM1)
390
0
42074
Swiss-Prot
-
MTKB_METEA
Methylorubrum extorquens (strain ATCC 14718 / DSM 1338 / JCM 2805 / NCIMB 9133 / AM1)
296
0
30519
Swiss-Prot
-
MTKA_RHILO
Mesorhizobium japonicum (strain LMG 29417 / CECT 9101 / MAFF 303099)
394
0
42482
Swiss-Prot
Secretory Pathway (Reliability: 2)
A0A0A0HQV3_9RHOB
328
0
35371
TrEMBL
other Location (Reliability: 4)
A0A316FKJ2_9RHOB
399
0
42686
TrEMBL
Secretory Pathway (Reliability: 1)
A0A348W7S6_9RHOB
253
0
27558
TrEMBL
Secretory Pathway (Reliability: 2)
A0A358HPS3_9PROT
389
0
41253
TrEMBL
Mitochondrion (Reliability: 5)
A0A3B9IFR0_9PROT
296
0
31568
TrEMBL
Secretory Pathway (Reliability: 2)
A0A4Q0M2A1_9HYPH
360
0
38128
TrEMBL
other Location (Reliability: 3)
A0A5A7N2W0_9PROT
297
0
31718
TrEMBL
Secretory Pathway (Reliability: 5)
A0A6B0Y425_9RHOB
313
0
33607
TrEMBL
Secretory Pathway (Reliability: 2)
A0A7Z0I2U2_9RHOB
396
0
41754
TrEMBL
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
34000
-
2 * 34000 (alpha) + 2 * 42500 (beta), SDS-PAGE, the phosphoenzyme has an alpha2beta2 structure
42500
-
2 * 34000 (alpha) + 2 * 42500 (beta), SDS-PAGE, the phosphoenzyme has an alpha2beta2 structure
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
tetramer
tetramer
-
2 * 34000 (alpha) + 2 * 42500 (beta), SDS-PAGE, the phosphoenzyme has an alpha2beta2 structure
tetramer
-
2 * 34000 (alpha) + 2 * 42500 (beta), SDS-PAGE, the phosphoenzyme has an alpha2beta2 structure
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
the phosphorylated enzyme is acid labile and base stable
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
during purification and storage, the enzyme preparation is supplemented with 50 mM KCl and 1 mM DTT to achieve an optimal stabilization
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Friedrich, M.; Laderer, U.; Schink, B.
Fermentative degradation of glycolic acid by defined synthrophic cocultures
Arch. Microbiol.
156
398-404
1991
Methanogenic bacterium
-
brenda
Friedrich, M.; Schink, B.
Fermentative degradation of glyoxylate by a new strictly anaerobic bacterium
Arch. Microbiol.
156
392-397
1991
Bacteria, Bacteria PerGlx1
-
brenda
Willibald, B.; Boves, H.; Holler, E.
Preparative synthesis of beta-L-malyl-coenzyme A assisted by malyl-coenzyme A synthetase from Pseudomonas AM1
Anal. Biochem.
227
363-367
1995
Pseudomonas sp., Pseudomonas sp. AM1(2006)
brenda
Surendranathan, K.K.; Hersch, L.B.
Malate thiokinase. Evidence for a random site reaction mechanism
J. Biol. Chem.
258
3794-3798
1983
Pseudomonas sp., Pseudomonas sp. AM1(2006)
brenda
Hersh, L.B.; Surendranathan, K.K.
Reaction of malate thiokinase with methoxycarbonyl-CoA disulfide
J. Biol. Chem.
257
11633-11638
1982
Pseudomonas sp.
brenda
Hersh, L.B.; Peet, M.
Half-of-the-sites reactivity in the malate thiokinase reaction
J. Biol. Chem.
256
1732-1737
1981
Pseudomonas sp., Pseudomonas sp. MA
brenda
Elwell,M.; Hersh, L.B.
Substrate-dependent dissociation of malate thiokinase
J. Biol. Chem.
254
2434-2438
1979
Pseudomonas sp., Pseudomonas sp. MA
brenda
Hersh, L.B.
Malate thiokinase. The reaction mechanism as determined by initial rate studies
J. Biol. Chem.
249
6264-6271
1974
Pseudomonas sp., Pseudomonas sp. MA
brenda
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., Pseudomonas sp. MA
brenda
Wu, X.; Zhou, F.; Tu, G.; Zou, X.
Gene cloning, expression and characterization of malate-CoA ligase in the polymerization pathway of polymalic acid from Aureobasidium pullulans
Acta Microbiol. Sin.
54
919-925
2014
Aureobasidium pullulans, Aureobasidium pullulans CCTCC M2012223
brenda
EXTERNAL LINKS (specific for EC-Number 6.2.1.9)
html completed
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2026.1 (March 2026)
About BRENDA
Social media
Help
Survey
Download
Contribution
Legal
Curated at
Member of
![DSMZ Digital Diversity]()
![Global Core Biodata Resource]()
![ELIXIR Core Data Resource]()
![German Network for Bioinformatics Infrastructure]()
