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EC Number Substrates Commentary Substrates Organism Products Commentary (Products) Reversibility
Display the word mapDisplay the reaction diagram Show all sequences 6.2.1.55ATP + [SAMP1]-Gly-Gly + [protein]-L-lysine - Haloferax volcanii AMP + diphosphate + N6-[[SAMP1]-Gly-Gly]-[[protein]-L-lysine] - ?
Display the word mapDisplay the reaction diagram Show all sequences 6.2.1.55ATP + [SAMP1]-Gly-Gly + [protein]-L-lysine the enzyme is required for the formation of both SAMP1- and SAMP2-protein conjugates Haloferax volcanii AMP + diphosphate + N6-[[SAMP1]-Gly-Gly]-[[protein]-L-lysine] - ?
Display the word mapDisplay the reaction diagram Show all sequences 6.2.1.55ATP + [SAMP1]-Gly-Gly + [protein]-L-lysine Haloferax volcanii forms differential SAMP-conjugates in the presence of only a single E1 and in the absence of any apparent E2 or E3 homologues suggesting a streamlined ubiquitin-like system for protein conjugation Haloferax volcanii AMP + diphosphate + N6-[[SAMP1]-Gly-Gly]-[[protein]-L-lysine] - ?
Display the word mapDisplay the reaction diagram Show all sequences 6.2.1.55ATP + [SAMP1]-Gly-Gly + [protein]-L-lysine working model for archaea in which the E1-like UbaA and ubiquitin-like SAMP proteins function in both protein conjugation and sulfur transfer. In this model, UbaA catalyzes the adenylation of the C-terminal glycine of the SAMPs for their activation in protein conjugation. This adenylation would also activate SAMP1 and SAMP2 for their acceptance of sulfur as a C-terminal thiocarboxylate to serve as a sulfur carrier in MoCo biosynthesis and tRNA thiolation, respectively. During protein conjugation, a thioester intermediate is suggested to be formed between the active site Cys188 of UbaA and the C-terminal carboxyl group of the SAMPs. This prediction is based on: (i) the requirement of UbaA Cys188 for protein-conjugate formation, (ii) the conservation of UbaA Cys188 with the active site cysteine of E1-type enzymes known to form an E1-Ub thioester, and (iii) the detection of isopeptide (and not persulfide) bonds between the C-terminal carboxyl group of SAMP2 and the epsilon-amino group of lysine residues of target proteins. However, further studies are needed to demonstrate this intermediate. It is not clear whether UbaA forms a covalent intermediate with the SAMPs after their adenylation in the sulfur transfer pathways and what provides the activated source of sulfur for this putative thiocarboxylation reaction Haloferax volcanii AMP + diphosphate + N6-[[SAMP1]-Gly-Gly]-[[protein]-L-lysine] - ?
Display the word mapDisplay the reaction diagram Show all sequences 6.2.1.55ATP + [SAMP1]-Gly-Gly + [protein]-L-lysine - Haloferax volcanii YW1001 AMP + diphosphate + N6-[[SAMP1]-Gly-Gly]-[[protein]-L-lysine] - ?
Display the word mapDisplay the reaction diagram Show all sequences 6.2.1.55ATP + [SAMP1]-Gly-Gly + [protein]-L-lysine - Haloferax volcanii ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2 AMP + diphosphate + N6-[[SAMP1]-Gly-Gly]-[[protein]-L-lysine] - ?
Display the word mapDisplay the reaction diagram Show all sequences 6.2.1.55ATP + [SAMP1]-Gly-Gly + [protein]-L-lysine Haloferax volcanii forms differential SAMP-conjugates in the presence of only a single E1 and in the absence of any apparent E2 or E3 homologues suggesting a streamlined ubiquitin-like system for protein conjugation Haloferax volcanii DSM 3757 AMP + diphosphate + N6-[[SAMP1]-Gly-Gly]-[[protein]-L-lysine] - ?
Display the word mapDisplay the reaction diagram Show all sequences 6.2.1.55ATP + [SAMP1]-Gly-Gly + [protein]-L-lysine the enzyme is required for the formation of both SAMP1- and SAMP2-protein conjugates Haloferax volcanii DSM 3757 AMP + diphosphate + N6-[[SAMP1]-Gly-Gly]-[[protein]-L-lysine] - ?
Display the word mapDisplay the reaction diagram Show all sequences 6.2.1.55ATP + [SAMP1]-Gly-Gly + [protein]-L-lysine working model for archaea in which the E1-like UbaA and ubiquitin-like SAMP proteins function in both protein conjugation and sulfur transfer. In this model, UbaA catalyzes the adenylation of the C-terminal glycine of the SAMPs for their activation in protein conjugation. This adenylation would also activate SAMP1 and SAMP2 for their acceptance of sulfur as a C-terminal thiocarboxylate to serve as a sulfur carrier in MoCo biosynthesis and tRNA thiolation, respectively. During protein conjugation, a thioester intermediate is suggested to be formed between the active site Cys188 of UbaA and the C-terminal carboxyl group of the SAMPs. This prediction is based on: (i) the requirement of UbaA Cys188 for protein-conjugate formation, (ii) the conservation of UbaA Cys188 with the active site cysteine of E1-type enzymes known to form an E1-Ub thioester, and (iii) the detection of isopeptide (and not persulfide) bonds between the C-terminal carboxyl group of SAMP2 and the epsilon-amino group of lysine residues of target proteins. However, further studies are needed to demonstrate this intermediate. It is not clear whether UbaA forms a covalent intermediate with the SAMPs after their adenylation in the sulfur transfer pathways and what provides the activated source of sulfur for this putative thiocarboxylation reaction Haloferax volcanii DSM 3757 AMP + diphosphate + N6-[[SAMP1]-Gly-Gly]-[[protein]-L-lysine] - ?
Display the word mapDisplay the reaction diagram Show all sequences 6.2.1.55ATP + [SAMP1]-Gly-Gly + [UbaA]-L-cysteine - Haloferax volcanii AMP + diphosphate + N6-[[SAMP1]-Gly-Gly]-[[UbaA]-L-cysteine] - ?
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