2.3.3.9: malate synthase
This is an abbreviated version!
For detailed information about malate synthase, go to the full flat file.
Word Map on EC 2.3.3.9
-
2.3.3.9
-
isocitrate
-
peroxisomal
-
icl
-
glyoxysomal
-
catalase
-
citrate
-
tricarboxylic
-
tuberculosis
-
shunt
-
cotyledons
-
seedling
-
microbodies
-
cucumber
-
gluconeogenesis
-
beta-oxidation
-
4.1.3.1
-
anaplerotic
-
fumarase
-
thiolase
-
cucumis
-
phosphotransacetylase
-
trosy
-
hydroxypyruvate
-
acetate-grown
-
agriculture
-
3-ketoacyl-coa
-
pumpkin
- 2.3.3.9
- isocitrate
- peroxisomal
- icl
- glyoxysomal
- catalase
- citrate
-
tricarboxylic
- tuberculosis
-
shunt
- cotyledons
- seedling
- microbodies
- cucumber
-
gluconeogenesis
-
beta-oxidation
-
4.1.3.1
-
anaplerotic
- fumarase
-
thiolase
-
cucumis
- phosphotransacetylase
-
trosy
- hydroxypyruvate
-
acetate-grown
- agriculture
- 3-ketoacyl-coa
-
pumpkin
Reaction
Synonyms
EC 4.1.3.2, GCE, GCE(13-573), glcB, glyoxylate cycle enzyme, glyoxylate transacetase, glyoxylic transacetase, L-malate glyoxylate-lyase (CoA-acetylating), malate synthase, malate synthase 1, malate synthase A, malate synthase G, malate synthase H, malate synthetase, malic synthetase, malic-condensing enzyme, MLS, MSA, MSG, MSH, SSO1334
ECTree
Advanced search results
Reaction
Reaction on EC 2.3.3.9 - malate synthase
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
acetyl-CoA + glyoxylate + H2O = (S)-malate + CoA
sequential bireactant mechanism
-
acetyl-CoA + glyoxylate + H2O = (S)-malate + CoA
sequencial random mechanism
-
acetyl-CoA + glyoxylate + H2O = (S)-malate + CoA
compulsory-order mechanism, glyoxylate being the first-binding substrate, glyoxylate triggers a conformational change in the enzyme and as a consequence, the correctly shaped binding site for acetyl-CoA is created
-
acetyl-CoA + glyoxylate + H2O = (S)-malate + CoA
mechanism: D631 and R338 act in concert to form the enolate anion of acetyl-CoA in the rate limiting step. C617 is oxidized to cysteine-sulfenic acid
-