Literature summary extracted from
Liu, Y.; Feng, Y.; Wang, Y.; Li, X.; Cao, X.; Xue, S.
Structural and biochemical characterization of MCAT from photosynthetic microorganism Synechocystis sp. PCC 6803 reveal its stepwise catalytic mechanism (2015), Biochem. Biophys. Res. Commun., 457, 398-403.
Cloned(Commentary)
EC Number |
Cloned (Comment) |
Organism |
---|
2.3.1.39 |
gene fabD, recombinant expression of wild-type and mutant enzymes in Escherichia coli strain BL21(DE3) |
Synechocystis sp. |
Protein Variants
EC Number |
Protein Variants |
Comment |
Organism |
---|
2.3.1.39 |
F187A |
site-directed mutagenesis, the mutant shows loss of about 65-70% activity compared to the wild-type enzyme |
Synechocystis sp. |
2.3.1.39 |
H188A |
site-directed mutagenesis, inactive mutant |
Synechocystis sp. |
2.3.1.39 |
H87A |
site-directed mutagenesis, the mutant shows loss of about 80% activity compared to the wild-type enzyme |
Synechocystis sp. |
2.3.1.39 |
Q10A |
site-directed mutagenesis, the mutant shows loss of about 70% activity compared to the wild-type enzyme |
Synechocystis sp. |
2.3.1.39 |
R113A |
site-directed mutagenesis, inactive mutant |
Synechocystis sp. |
2.3.1.39 |
S88T |
site-directed mutagenesis, the mutant initializes the reaction by H87 deprotonating S88T which is different from the wild-type, loss of 10% activity compared to the wild-type enzyme |
Synechocystis sp. |
2.3.1.39 |
T56A |
site-directed mutagenesis, the mutant shows loss of about 60% activity compared to the wild-type enzyme |
Synechocystis sp. |
Natural Substrates/ Products (Substrates)
EC Number |
Natural Substrates |
Organism |
Comment (Nat. Sub.) |
Natural Products |
Comment (Nat. Pro.) |
Rev. |
Reac. |
---|
2.3.1.39 |
malonyl-CoA + an [acyl-carrier protein] |
Synechocystis sp. |
- |
CoA + a malonyl-[acyl-carrier protein] |
- |
? |
|
Organism
EC Number |
Organism |
UniProt |
Comment |
Textmining |
---|
2.3.1.39 |
Synechocystis sp. |
P73242 |
gene fabD or slr2023 |
- |
Reaction
EC Number |
Reaction |
Comment |
Organism |
Reaction ID |
---|
2.3.1.39 |
malonyl-CoA + an [acyl-carrier protein] = CoA + a malonyl-[acyl-carrier protein] |
residues Arg113, Ser88 and His188 constitute the enzyme's catalytic triad, catalytic mechanism, detailed overview. Malonyl-CoA binds to MCAT, involving Ser88, Arg113, Met117 and Phe187. The second step forming an ACP-MCAT-malonyl intermediate is rate-limiting instead of the malonyl-CoA-MCAT intermediate formed in the first step. His87, Arg113 and Ser88 render different contributions for the two intermediates |
Synechocystis sp. |
|
Substrates and Products (Substrate)
EC Number |
Substrates |
Comment Substrates |
Organism |
Products |
Comment (Products) |
Rev. |
Reac. |
---|
2.3.1.39 |
malonyl-CoA + an [acyl-carrier protein] |
- |
Synechocystis sp. |
CoA + a malonyl-[acyl-carrier protein] |
- |
? |
|
Synonyms
EC Number |
Synonyms |
Comment |
Organism |
---|
2.3.1.39 |
malonyl-coenzyme A: acyl-carrier protein transacylase |
- |
Synechocystis sp. |
2.3.1.39 |
MCAT |
- |
Synechocystis sp. |
General Information
EC Number |
General Information |
Comment |
Organism |
---|
2.3.1.39 |
additional information |
residues Arg113, Ser88 and His188 constitute cthe enzyme's atalytic triad. Structure homology modeling by molecular replacement using the enzyme from Escherichia coli, PDB: 1MLA, as a search model |
Synechocystis sp. |