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EC Number General Information Commentary Reference
Show all pathways known for 2.3.1.129Display the word mapDisplay the reaction diagram Show all sequences 2.3.1.129evolution the enzymes in early lipid A biosynthesis are highly conserved in gram-negative pathogens. LpxA and LpxD are structurally homologous possessing the unique left-handed beta-helix fold, which stems from an extensive hexapeptide repeat motif in their respective primary amino acid sequences 718571
Show all pathways known for 2.3.1.129Display the word mapDisplay the reaction diagram Show all sequences 2.3.1.129evolution the overall structure of AtLpxA is very similar to that of Escherichia coli LpxA, EcLpxA, with an alpha-helical-rich C-terminus and characteristic N-terminal left-handed parallel beta-helix. All key catalytic and chain length determining residues of EcLpxA are conserved in AtLpxA,but AtLpxA has an additional coil and loop added to the N-terminal left-handed parallel beta-helix not seen in EcLpxA 718930
Show all pathways known for 2.3.1.129Display the word mapDisplay the reaction diagram Show all sequences 2.3.1.129metabolism acyltransferases LpxA and LpxD catalyze functionally similar acylations of their respective UDP-glucosamine-based substrates using R-3-hydroxymyristoyl-ACP as the acyl donor in the Kdo2-lipid A biosynthesis in Escherichia coli 718462
Show all pathways known for 2.3.1.129Display the word mapDisplay the reaction diagram Show all sequences 2.3.1.129metabolism LpxA catalyzes the first step in lipid A biosynthesis, pathway overview 720913
Show all pathways known for 2.3.1.129Display the word mapDisplay the reaction diagram Show all sequences 2.3.1.129metabolism LpxA is the first enzyme in the biosynthetic pathway for the Lipid A component of the outer membrane lipopolysaccharide 720069
Show all pathways known for 2.3.1.129Display the word mapDisplay the reaction diagram Show all sequences 2.3.1.129metabolism UDP-N-acetylglucosamine acyltransferase, LpxA, catalyzes the first step of lipid A biosynthesis 718571
Show all pathways known for 2.3.1.129Display the word mapDisplay the reaction diagram Show all sequences 2.3.1.129more active site structure of AtLpxA, overview 718930
Show all pathways known for 2.3.1.129Display the word mapDisplay the reaction diagram Show all sequences 2.3.1.129more UDP-N-acetylglucosamine 3-O-acyltransferase is a protein with a left-handed parallel beta-helix, which is a natural nanotube associated with unusual high stability, molecular dynamics simulations using LpxA crystal structure, PDB ID 1LXA, and formation of a dynamical cross-correlation map, overview. Construction of the unfolding conformational energy landscape identifies the probable intermediates that can appear in the unfolding pathway of the protein, unfolding kinetics of the three-stranded beta-sheet protein, overview 719101
Show all pathways known for 2.3.1.129Display the word mapDisplay the reaction diagram Show all sequences 2.3.1.129physiological function acyl-carrier protein (ACP), a small 8-10 kDa component of the type II dissociated fatty acid synthase system, of Vibrio harveyi interacts with LpxA and induces ACP-folding 691096
Show all pathways known for 2.3.1.129Display the word mapDisplay the reaction diagram Show all sequences 2.3.1.129physiological function enzyme interacts with virulence factor CSK29544_02616, i.e. Labp. Labp increases the enzymatic activity of LpxA without influencing its expression 758442
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