EC Number   |
General Information |
Reference |
|---|
   3.4.21.53 | evolution |
although Lon is originally identified as an ATP-dependent protease with fused AAA+ (ATPases associated with diverse cellular activities) and protease domains, analyses have recently identified LonC as a class of Lon-like proteases with no intrinsic ATPase activity. In contrast to the canonical ATP-dependent Lon present in eukaryotic organelles and prokaryotes, LonC contains an AAA-like domain that lacks the conserved ATPase motifs |
731056 |
| 3.4.21.53 | evolution |
evolution has diversified rather than optimized the protein unfolding activities of different AAA+ proteases, Escherichia coli utilizes five different AAA+ proteases: Lon, ClpXP, ClpAP, HslUV, and FtsH |
732882 |
| 3.4.21.53 | evolution |
homooligomeric ATP-dependent LonA proteases are bifunctional enzymes belonging to the superfamily of AAA+ proteins |
732906 |
| 3.4.21.53 | evolution |
human enzyme hLon and Escherichia coli enzyme ELon bind to ADP and undergo at least one structural change that exposes the same tryptic digestion site, suggesting the presence of at least one conserved structural change in the two enzyme homologues upon binding to ADP |
753692 |
| 3.4.21.53 | evolution |
human Lon (hLon) is a mitochondrial AAA+ protein (ATPases associated with diverse cellular activities) belonging to the LonA protease subfamily |
755444 |
| 3.4.21.53 | evolution |
Lon is a highly conserved member of the AAA+ (ATPases associated with diverse cellular activities) protease family |
755340 |
| 3.4.21.53 | evolution |
Lon proteases can be divided into two subfamilies: LonA (found in eubacteria and eukarya) and LonB (found in archaea). LonA proteases are formed by three functional domains: the N-terminal, involved in substrate binding, the central AAA+ domain, and the C-terminal domain (named P domain), which containing the Ser-Lys catalytic dyad for proteolytic activity. LonB proteases are composed by an ATPase and a protease domain and a hydrophobic transmembrane region which anchors the protein to the internal face of cell membrane |
752803 |
| 3.4.21.53 | evolution |
Lon proteases can be divided into two subfamilies: LonA (found in eubacteria and eukarya) and LonB (found in archaea). LonA proteases are formed by three functional domains: the N-terminal, involved in substrate binding, the central AAA+ domain, and the C-terminal domain (named P domain), which containing the Ser-Lys catalytic dyad for proteolytic activity. LonB proteases are composed by an ATPase and a protease domain and a hydrophobic transmembrane region which anchors the protein to the internal face of cell membrane. In eukarya, two Lon proteases are present: a mitochondrial and a peroxisomal form, encoded by two different genes |
-, 752803 |
| 3.4.21.53 | evolution |
LonA from Escherichia coli belongs to the superfamily of AAA+ proteins, family S16 of proteases. The presence of an extended variable N-terminal region preceding the AAA+ modules is a characteristic feature of LonA proteases distinguishing them from other AAA+ proteins |
755391 |
| 3.4.21.53 | evolution |
phylogenetic analysis reveals that Lon-like-Ms and its homologs are members of the Lon family. The ATP-dependent Lon (La) protease is the most highly conserved member of the energy-dependent protease present in the cytosol of prokaryotes and in the mitochondria and peroxisomes of eukaryotes. While the LonA group is found in eukaryotes and bacteria, the LonB subfamily proteins are only found in archaea. Two genes (Msm 1569 and Msm 1754) encoding Lon occur in the genome sequence, and the encoded proteins may play different roles. Msm 1569 encodes a canonical LonB protease (Lon-Ms). Msm 1754 (Lon-like-Ms) differs considerably from previously reported Lon proteases |
-, 752612 |
