Any feedback?
Please rate this page
(enzyme.php)
(0/150)

BRENDA support

BRENDA Home
show all | hide all No of entries

Information on EC 2.3.3.9 - malate synthase and Organism(s) Haloferax volcanii and UniProt Accession D4GTL2

for references in articles please use BRENDA:EC2.3.3.9
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
     2 Transferases
         2.3 Acyltransferases
             2.3.3 Acyl groups converted into alkyl groups on transfer
                2.3.3.9 malate synthase
IUBMB 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.
Specify your search results
Select one or more organisms in this record: ?
This record set is specific for:
Haloferax volcanii
UNIPROT: D4GTL2
Show additional data
Do not include text mining results
Include (text mining) results
Include results (AMENDA + additional results, but less precise)
Word Map
The taxonomic range for the selected organisms is: Haloferax volcanii
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
malate synthase, malate synthase g, glyoxylate cycle enzyme, malate synthetase, malate synthase a, malate synthase 1, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malate synthase A
isoform
malate synthase G
isoform
malate synthase H
isoform
glyoxylate transacetase
-
-
-
-
glyoxylic transacetase
-
-
-
-
L-malate glyoxylate-lyase (CoA-acetylating)
-
-
-
-
malate synthase 1
-
-
-
-
malate synthase G
-
-
-
-
malate synthetase
-
-
-
-
malic synthetase
-
-
-
-
malic-condensing enzyme
-
-
-
-
MSG
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
aldol condensation
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
acetyl-CoA:glyoxylate C-acetyltransferase (thioester-hydrolysing, carboxymethyl-forming)
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.
CAS REGISTRY NUMBER
COMMENTARY hide
9013-48-3
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
glyoxylate + acetyl-CoA + H2O
(S)-malate + CoA
show the reaction diagram
-
-
-
?
acetyl-CoA + H2O + glyoxylate
(S)-malate + CoA
show the reaction diagram
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
acetyl-CoA + H2O + glyoxylate
(S)-malate + CoA
show the reaction diagram
-
key enzyme of the glyoxylate cycle enzyme
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Mg2+
contains one Mg2+ ion in the active site
KCl
-
salt optimum: 3.0 M KCl
Mg2+
-
activity is dependent on Mg2+
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.00012
acetyl-CoA
-
pH 8.0, 40°C
0.00011
glyoxylate
-
pH 8.0, 40°C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
8
-
assay at
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7 - 10
-
pH 7.0: about 40% of maximal activity, pH 10.0: about 45% of maximal activity
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
40
-
assay at
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
25 - 80
-
25°C: about 45% of maximal activity, 80°C: about 45% of maximal activity
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
UniProt
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
no activity can be detected when lactate is the carbon source, but high activity is measured when acetate is
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
-
key enzyme of the glyoxylate cycle enzyme
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
200000
-
gel filtration
67000
-
3 * 67000, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
malate synthase isoforms A and G
trimer or hexamer
malate synthase isoform H is found in the native state as a trimer/hexamer equilibrium
homotrimer
-
3 * 67000, SDS-PAGE
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
malate synthase isoform H in complex with glyoxylate and also as a ternary complex with acetyl-coenzyme A and pyruvate, sitting drop vapor diffusion method, using 0.17 M ammonium acetate, 24.5-27% (w/v) PEG 4500, 15% (v/v) glycerol, and 0.085 M sodium acetate trihydrate at a pH of 4.4-5.0
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
reverse phase chromatography, anion-exchange column chromatography, and gel filtration
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Bracken, C.D.; Neighbor, A.M.; Lamlenn, K.K.; Thomas, G.C.; Schubert, H.L.; Whitby, F.G.; Howard, B.R.
Crystal structures of a halophilic archaeal malate synthase from Haloferax volcanii and comparisons with isoforms A and G
BMC Struct. Biol.
11
23
2011
Haloferax volcanii (D4GTL2), Haloferax volcanii
Manually annotated by BRENDA team
Serrano, J.A.; Camacho, M.; Bonete, M.J.
Operation of glyoxylate cycle in halophilic archaea: presence of malate synthase and isocitrate lyase in Haloferax volcanii
FEBS Lett.
434
13-16
1998
Haloferax volcanii, Haloferax volcanii DSM 3757
Manually annotated by BRENDA team