EC Number   |
Reaction |
Reference |
|---|
    2.3.1.169 | acetyl-CoA + a [Co(I) corrinoid Fe-S protein] = CO + CoA + a [methyl-Co(III) corrinoid Fe-S protein] |
chemical steps and conformational changes in the mechanism of acetyl-CoA synthase, overview |
-, 719862 |
| 2.3.1.169 | acetyl-CoA + a [Co(I) corrinoid Fe-S protein] = CO + CoA + a [methyl-Co(III) corrinoid Fe-S protein] |
CO migrates to the A-cluster through two pathways, one involving and one not involving the tunnel |
687824 |
| 2.3.1.169 | acetyl-CoA + a [Co(I) corrinoid Fe-S protein] = CO + CoA + a [methyl-Co(III) corrinoid Fe-S protein] |
CoA is the last substrate to bind and CO and the methyl group bind randomly as the first substrate in acetyl-CoA synthesis |
687803 |
| 2.3.1.169 | acetyl-CoA + a [Co(I) corrinoid Fe-S protein] = CO + CoA + a [methyl-Co(III) corrinoid Fe-S protein] |
Enzyme accepts the methyl group from the methylated corrinoid/iron-sulfur protein, binds a carbonyl group from CO, CO2, or the carboxyl of pyruvate, and binds coenzyme A. Then the enzyme catalyses the synthesis of acetyl-CoA from these enzyme bound groups. Additionally the enzyme catalyses two exchange reactions between the methylated corrinoid/iron-sulfur protein and methylated enzyme and between methylated enzyme and the methyl moiety of acetyl-CoA. |
390475, 644850 |
| 2.3.1.169 | acetyl-CoA + a [Co(I) corrinoid Fe-S protein] = CO + CoA + a [methyl-Co(III) corrinoid Fe-S protein] |
enzyme contains binding sites for the methyl, carbonyl, and CoA moieties of acetyl-CoA and catalyses the assembly of acetyl-CoA from these enzyme-bound groups, under optimal conditions the rate-limiting step involves methylation of enzyme by the methylated corrinoid/iron-sulfur protein |
644674 |
| 2.3.1.169 | acetyl-CoA + a [Co(I) corrinoid Fe-S protein] = CO + CoA + a [methyl-Co(III) corrinoid Fe-S protein] |
investigation of putative intermediate states from the catalytic cycle by hybrid density functional theory. A mononuclear mechanism in which CO and CH3 bind the proximal nickel is favored over the binuclear mechanism in which CO and CH3 bind the proximal and distal nickel ions resp. The formation of a disulfide bond in the active site could provide the two electrons necessary for the reaction if methylation occurs simultaneously. The crystallographic closed form of the active site needs to open to accomodate ligands in the equatorial state |
674161 |
| 2.3.1.169 | acetyl-CoA + a [Co(I) corrinoid Fe-S protein] = CO + CoA + a [methyl-Co(III) corrinoid Fe-S protein] |
kinetics of methyl group transfer between the cobalt of the corrinoid/iron-sulfur protein and the nickel of Ni-X-Fe4S4 cluster, called the A-cluster of enzyme, the reaction is reversible |
644861 |
| 2.3.1.169 | acetyl-CoA + a [Co(I) corrinoid Fe-S protein] = CO + CoA + a [methyl-Co(III) corrinoid Fe-S protein] |
pathway |
390465, 390475, 644674, 644850, 644855, 644861, 644862 |
| 2.3.1.169 | acetyl-CoA + a [Co(I) corrinoid Fe-S protein] = CO + CoA + a [methyl-Co(III) corrinoid Fe-S protein] |
stopped-flow analysis of two steps within the catalytic cycle. Vast majority of enzymes within a population should be in the methylated form suggesting that the following CO insertion step is rate limiting. Reaction rate is most sensitively affected by a change in the rate coefficient associated with the CO insertion step |
674177 |
| 2.3.1.169 | acetyl-CoA + a [Co(I) corrinoid Fe-S protein] = CO + CoA + a [methyl-Co(III) corrinoid Fe-S protein] |
the corronoid protein functions as methyl group carrier during acetyl-CoA synthesis and decomposition |
390465 |
