EC Number   |
General Information |
Reference |
|---|
   2.3.1.B34 | evolution |
enzyme BsAcsA is a GCN5-related N-acetyltransferase and belongs to the GCN5-related N-acetyltransferase (GNAT) protein superfamily (PF00583), all sharing a core catalytic domain despite low sequence homology. BsAcuA is a type-IV bGNAT enzyme |
-, 755801 |
| 2.3.1.B34 | evolution |
enzyme SaAcuA is a GCN5-related N-acetyltransferase and belongs to the GCN5-related N-acetyltransferase (GNAT) protein superfamily (PF00583), all sharing a core catalytic domain despite low sequence homology. SaAcuA is a type-IV bGNAT enzyme |
-, 755801 |
| 2.3.1.B34 | evolution |
enzyme SePat is a GCN5-related N-acetyltransferase and belongs to the GCN5-related N-acetyltransferase (GNAT) protein superfamily (PF00583), all sharing a core catalytic domain despite low sequence homology. SePat is a two-domain bGNAT that belongs to type I |
-, 755801 |
| 2.3.1.B34 | evolution |
the enzyme belongs to the GCN5-related N-acetyltransferases family (GNAT) is an important family of proteins that includes more than 100000 members among eukaryotes and prokaryotes |
-, 756044 |
| 2.3.1.B34 | metabolism |
enzyme acetylation by Pat is reversed by deacetylase enzymes, including the NAD+-dependent sirtuin-like deacetylases, which allows for the rapid response and adaptation to new metabolic needs or physiological changes |
-, 756044 |
| 2.3.1.B34 | metabolism |
enzyme acetylation by Pat is reversed by deacetylase enzymes, including the NAD+-dependent sirtuin-like deacetylases, which allows for the rapid response and adaptation to new metabolic needs or physiological changes. The ACS gene and AcuABC operon are adjacent to each other, with AcuA functioning as the acetylase and AcuC as an NAD+-independent deacetylase |
-, 756044 |
| 2.3.1.B34 | metabolism |
inactive SaAcsAc is deacetylated (hence reactivated) by the NAD+-dependent (class III) sirtuin protein deacetylase (hereafter SaCobB). In vivo and in vitro evidence show that SaAcuA and SaCobB modulate the level of SaAcs activity in Staphylococcus aureus |
-, 755801 |
| 2.3.1.B34 | more |
key determinants for protein substrate recognition and subsequent acetylation. In addition to the conserved PX4GK motif on the C-terminus of the ACS protein substrate, a trio of arginines located after the PX4GK motif also conserved in ACS homologues was shown to interact with a negative patch on Pat. Those complementary ionic interactions contribute to Pat substrate specificity |
-, 756044 |
| 2.3.1.B34 | physiological function |
enzyme PatA acetylates acetoacetyl-CoA synthase AacS at the active-site residue Lys617 and acetylation inactivates AacS. Acetylated AacS is deacetylated by a sirtuin-type protein deacetylase |
-, 728335 |
| 2.3.1.B34 | physiological function |
Gcn5-like protein acetyltransferase AcuA is the enzyme responsible for the acetylation of the AMP-forming acetyl coenzyme A synthetase AcsA. Acetylated AcsA is deacetylated by a sirtuin-type NAD+-dependent consuming deacetylase SrtN |
-, 736362 |
