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Results 1 - 10 of 18 > >>
EC Number General Information Commentary Reference
Display the word mapDisplay the reaction diagram Show all sequences 6.3.1.19evolution PafA is a member of the glutamine synthetase (GS) family of proteins -, 745678
Display the word mapDisplay the reaction diagram Show all sequences 6.3.1.19evolution the Pup-proteasome system (PPS) is functionally related to the eukaryotic Ub-proteasome system, but the number of the involved players is smaller, comparison of reaction mechanisms, overview -, 745555
Display the word mapDisplay the reaction diagram Show all sequences 6.3.1.19evolution the Pup-proteasome system (PPS) is functionally related to the eukaryotic Ub-proteasome system, but the number of the involved players is smaller, comparison of reaction mechanisms, overview. Intrinsically disordered Pup is structurally unlike the stably folded ubiquitin -, 745555
Display the word mapDisplay the reaction diagram Show all sequences 6.3.1.19malfunction in a pafA knockout strain pupylated proteins are undetectable and proteasomal substrate proteins accumulate -, 729308
Display the word mapDisplay the reaction diagram Show all sequences 6.3.1.19metabolism posttranslational regulation of coordinated enzyme activities in the prokaryotic ubiquitin-like protein (Pup)-proteasome system (PPS), overview. Pup, a ubiquitin analogue, is conjugated to proteins through the activities of two enzymes, Dop (deamidase of Pup) and PafA (proteasome accessory factor A), the Pup ligase. The depupylase activity of Dop counteracts the actions of PafA. tight Pup binding and the limited degree of Dop interaction with high-molecular-weight pupylated proteins results in preferred Pup deamidation over protein depupylation by enzyme Dop. Dop is depleted in the absence of Pup in stationary-phase cells. Pup-PanB and Pup-IdeR act as tight-binding competitors versus Pup binding by Dop. Pup binding stabilizes Dop and prevents its depletion. PafA and Dop generate a high-molecular-weight pupylome -, 746316
Display the word mapDisplay the reaction diagram Show all sequences 6.3.1.19metabolism prokaryotic ubiquitin-like protein (Pup) is a post-translational modifier that attaches to more than 50 proteins in Mycobacteria. Proteasome accessory factor A (PafA) is responsible for Pup conjugation to substrates -, 729641
Display the word mapDisplay the reaction diagram Show all sequences 6.3.1.19metabolism proteasome-containing bacteria possess a tagging system that directs proteins to proteasomal degradation by conjugating them to a prokaryotic ubiquitin-like protein (Pup). A single ligating enzyme, PafA, is responsible for Pup conjugation to lysine side chains of protein substrates. As Pup is recognized by the regulatory subunit of the proteasome, Pup functions as a degradation tag. Ligating enzyme PafA and the proteasome can function as a modular machine for the tagging and degradation of cytoplasmic proteins -, 729245
Display the word mapDisplay the reaction diagram Show all sequences 6.3.1.19metabolism pupylation is a bacterial post-translational modification of target proteins on lysine residues with prokaryotic ubiquitinlike protein (Pup). Pup-tagged substrates are recognized by a proteasome-interacting ATPase (Mpa) in Mycobacterium tuberculosis. Mpa unfolds pupylated substrates and threads them into the proteasome core particle for degradation -, 730004
Display the word mapDisplay the reaction diagram Show all sequences 6.3.1.19metabolism pupylation is a posttranslational protein modification occurring in mycobacteria and other actinobacteria that is functionally analogous to ubiquitination -, 730443
Display the word mapDisplay the reaction diagram Show all sequences 6.3.1.19physiological function bacteria use an intrinsically disordered protein, Pup, to mark proteins for destruction. The protein degradation machinery of Mycobacterium tuberculosis includes a proteasome and a ubiquitin-like protein (Pup). Proteasome accessory factor A (PafA) attaches Pup to proteins to target them for degradation by the proteasome. PafA can move Pup from one proteasome substrate, inositol 1-phosphate synthetase (Ino1), to two different proteins, malonyl coenzyme A (CoA)-acyl carrier protein transacylase (FabD) and lonely guy (Log). This apparent transpupylation reaction requires a previously unrecognized depupylase activity in PafA, and, surprisingly, this depupylase activity is much more efficient than the activity of the dedicated depupylase Dop (deamidase of Pup). Thus, PafA can potentially use both newly synthesized Pup and recycled Pup to doom proteins for degradation. In contrast, enzyme Dop, in addition to deamidating PupGln to PupGlu, can remove Pup from proteins, which can rescue them from proteasomal degradation. PafA, unlike Dop, can-not deamidate PupGln to PupGlu, thus, PafA amidase activity appears to be limited to pupylated proteins -, 745678
Results 1 - 10 of 18 > >>