| RRC ID |
66209
|
| Author |
Huergo LF, Araújo GAT, Santos ASR, Gerhardt ECM, Pedrosa FO, Souza EM, Forchhammer K.
|
| Title |
The NADP-dependent malic enzyme MaeB is a central metabolic hub controlled by the acetyl-CoA to CoASH ratio.
|
| Journal |
Biochim Biophys Acta Proteins Proteom
|
| Abstract |
Malic enzymes participate in key metabolic processes, the MaeB-like malic enzymes carry a catalytic inactive phosphotransacetylase domain whose function remains elusive. Here we show that acetyl-CoA directly binds and inhibits MaeB-like enzymes with a saturable profile under physiological relevant acetyl-CoA concentrations. A MaeB-like enzyme from the nitrogen-fixing bacterium Azospirillum brasilense, namely AbMaeB1, binds both acetyl-CoA and unesterified CoASH in a way that inhibition of AbMaeB1 by acetyl-CoA is relieved by increasing CoASH concentrations. Hence, AbMaeB1 senses the acetyl-CoA/CoASH ratio. We revisited E. coli MaeB regulation to determine the inhibitory constant for acetyl-CoA. Our data support that the phosphotransacetylase domain of MaeB-like enzymes senses acetyl-CoA to dictate the fate of carbon distribution at the phosphoenol-pyruvate / pyruvate / oxaloacetate metabolic node.
|
| Volume |
1868(9)
|
| Pages |
140462
|
| Published |
2020-9-1
|
| DOI |
10.1016/j.bbapap.2020.140462
|
| PII |
S1570-9639(20)30109-6
|
| PMID |
32485238
|
| MeSH |
Acetyl Coenzyme A / metabolism*
Azospirillum brasilense / genetics
Azospirillum brasilense / metabolism
Bacteria / metabolism
Coenzyme A / metabolism*
Escherichia coli / genetics
Escherichia coli / metabolism
Malate Dehydrogenase / genetics
Malate Dehydrogenase / metabolism*
Malates / metabolism*
NADP / metabolism*
Phosphate Acetyltransferase / metabolism
|
| IF |
2.609
|
| Resource |
| Prokaryotes E. coli |
ASKA collection |
