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Results 1 - 10 of 11 > >>
EC Number General Information Commentary Reference
Show all pathways known for 2.5.1.17Display the word mapDisplay the reaction diagram Show all sequences 2.5.1.17evolution ATP:co(I)rrinoid adenosyltransferases, ACATs, are separated into three families namely, CobA, EutT, and PduO 721682
Show all pathways known for 2.5.1.17Display the word mapDisplay the reaction diagram Show all sequences 2.5.1.17evolution cob(I)alamin adenosyltransferases are separated into three type groups according to their amino acid sequences: CobA, PduO, and EutT. Among these adenosyltransferases, the PduO-type adenosyltransferases are the most widely distributed enzyme type. Whereas the CobA-type enzyme, which is constitutively expressed, is encoded by the cobA gene, PduO and EutT-type adenosyltransferases are encoded within large operons whose functions are required for the catabolism of 1,2-propanediol or ethanolamine. Despite the fact that all three families of adenosyltransferases catalyze the same overall reaction, they share little sequence identity of below 20% and the CobA and PduO enzymes have fairly different three-dimensional structures 721492
Show all pathways known for 2.5.1.17Display the word mapDisplay the reaction diagram Show all sequences 2.5.1.17malfunction a HH103 cobO mutant (strain SVQ524), is constructed by the insertion of omega interposon in the BglII site of cobO gene. Mutant is auxotroph for methionine and cobalamin as it is shown that the presence of either compound restores the growth on minimal medium. Mutant SVQ524 fails to nodulate on Vigna radiate but is able to nodulate on Glycine max cvs. Williams and Peking and Cajanus cajan. The roots of mutant plants do not secrete enough cobalamin and/or methionine to support growth of cobalamin/methionine auxotrophs in the rhizosphere. The phenotype of SVQ524 is rescued by the addition of methionine or cobalamin to the plant growth media or by the presence of a copy of the cobO gene 701946
Show all pathways known for 2.5.1.17Display the word mapDisplay the reaction diagram Show all sequences 2.5.1.17malfunction a methionine and cobalamin mutant strain (SVQ336) of Sinorhizobium fredii HH103 is obtained by Tn5-lacZ mutagenesis. Sequence analysis show that the transposon is inserted into a gene homologous to cobO. cobO mutant SVQ336 is auxotroph for methionine and cobalamin as it is shown that the presence of either compound restores the growth of SVQ336 on minimal medium 701946
Show all pathways known for 2.5.1.17Display the word mapDisplay the reaction diagram Show all sequences 2.5.1.17metabolism the enzyme is involved in 1,2-propanediol utilization 759238
Show all pathways known for 2.5.1.17Display the word mapDisplay the reaction diagram Show all sequences 2.5.1.17metabolism the enzyme is involved in de novo adenosylcobamide biosynthesis, and in salvaging complete and incomplete corrinoids from the environment -, 758817
Show all pathways known for 2.5.1.17Display the word mapDisplay the reaction diagram Show all sequences 2.5.1.17metabolism the enzyme is involved in the de novo synthesis and scavenging of corrinoids to maintain adequate cellular levels of adenosylcobalamin, a biological cofactor used in a variety of enzyme-mediated organic rearrangement and elimination reactions 758818
Show all pathways known for 2.5.1.17Display the word mapDisplay the reaction diagram Show all sequences 2.5.1.17more active-site region of wild-type and mutant PduOs complexed with Co(II)Cbl and cosubstrate ATP, structure determination and modeling, overview 722386
Show all pathways known for 2.5.1.17Display the word mapDisplay the reaction diagram Show all sequences 2.5.1.17more residues Phe91 and Trp93 play a critical role in the mechanism of four-coordinate Cob(II)alamin formation in the active site of the Salmonella enterica ATP:Co(I)rrinoid adenosyltransferase enzyme, overview. The enzyme adopts a closed conformation and residues Phe91 and Trp93 displace 5,6-dimethylbenzimidazole, the lower nucleotide ligand base of cobalamin, to generate a transient four-coordinate cobalamin, which is critical in the formation of the AdoCbl Co-C bond, important role of bulky hydrophobic side chains in the active site. CobA increases the redox potential of the cob(II)alamin/cob(I)alamin couple to facilitate formation of the Co-C bond 721682
Show all pathways known for 2.5.1.17Display the word mapDisplay the reaction diagram Show all sequences 2.5.1.17more structural comparisons between apo BcPduO and BcPduO in complex with MgATP reveal that the N-terminal strands of both structures are ordered, which is in contrast with the most previously available PduO-type adenosyltransferase structures. Apo BcPduO is bound to additional dioxane molecules causing a side chain conformational change at the Tyr30 residue, which is an important residue that mediates hydrogen bonding with ATP molecules upon binding of cobalamin to the active site 721492
Results 1 - 10 of 11 > >>