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Results 1 - 6 of 6
EC Number General Information Commentary Reference
Show all pathways known for 2.7.1.29Display the word mapDisplay the reaction diagram Show all sequences 2.7.1.29evolution analysis of the glycerol metabolism genes in metagenomes suggests that Halorubrum and Haloquadratum possess mostly dihydroxyacetone kinase genes while Salinibacter possesses mostly glycerol-3-phosphate dehydrogenase genes. Family abundance of genes dhaL and dhaK, phylogenetic analysis. Across gene family, taxonomic affiliations of the dihydroxyacetone kinase families are closest to each other, as well as those of the alcohol dehydrogenase (Fe-ADH) and glycerol kinase (FGGY) gene families. Haloquadratum associates with dihydroxyacetone kinase gene families in the SS19, SS33, and SS37 metagenomes. By using the power of CRISPR spacers to link viruses to their prokaryotic hosts, the virus-host interactions in geographically diverse salterns are explored. Metagenomic CRISPRs detected with two independent methods map haloviruses to saltern hosts -, 759901
Show all pathways known for 2.7.1.29Display the word mapDisplay the reaction diagram Show all sequences 2.7.1.29evolution analysis of the glycerol metabolism genes in metagenomes suggests that Halorubrum and Haloquadratum possess mostly dihydroxyacetone kinase genes while Salinibacter possesses mostly glycerol-3-phosphate dehydrogenase genes. Family abundance of genes dhaL and dhaK, phylogenetic analysis. Across gene family, taxonomic affiliations of the dihydroxyacetone kinase families are closest to each other, as well as those of the alcohol dehydrogenase (Fe-ADH) and glycerol kinase (FGGY) gene families. Halorubrum associates with dihydroxyacetone kinase gene families in the IC21 and Cahuil metagenomes. By using the power of CRISPR spacers to link viruses to their prokaryotic hosts, the virus-host interactions in geographically diverse salterns are explored. Metagenomic CRISPRs detected with two independent methods map haloviruses to saltern hosts -, 759901
Show all pathways known for 2.7.1.29Display the word mapDisplay the reaction diagram Show all sequences 2.7.1.29metabolism anaerobic fermentative metabolism of glycerol. Proteome analysis as well as enzyme assays performed in cell-free extracts demonstrate that glycerol is degraded via glyceraldehyde-3-phosphate, which is further metabolized through the lower part of glycolysis leading to formation of mainly ethanol and hydrogen 748573
Show all pathways known for 2.7.1.29Display the word mapDisplay the reaction diagram Show all sequences 2.7.1.29more 1-propanol production from glycerol is achieved by addition of the ATP-dependent dihydroxyacetone kinase gene to Escherichia coli harboring pKK_mde and pRSF_pduCDEGOQS, reconstruction of the 1,2-propanediol (1,2-PD) synthetic pathway (pKK_mde) in Escherichia coli, pathway overview -, 759519
Show all pathways known for 2.7.1.29Display the word mapDisplay the reaction diagram Show all sequences 2.7.1.29more analysis of the reaction mechanism of the wild-type enzyme and the most active experimentally measured mutant (Glu526Lys) with polyphosphate as phosphoryl donor by use of hybrid quantum mechanics/molecular mechanics (QM/MM) potentials, with the QM region described by semiempirical and DFT methods. The initial coordinates of the protein and the phospholipid are taken from the X-ray structure of the apoform of enzyme DHAK from Citrobacter freundii (PDB ID 1UN8). The crystal structure contains two protein chains defined as chain A and chain B. Since the full structure is symmetric, a fragment of each chain is removed obtaining a two close domain structure where the chain A fragment corresponds to the DhaL domain, and the chain B to the DhaK-domain. Missing residues of the flexible loop of the L-domain are manually added within the help of Molden program. The coordinates of Dha and magnesium cations are taken from the PDB ID 1UN9 that corresponds to the Dha/ANP form. The ATP binding domain is a barrel composed by eight amphipathic alpha-helix stabilized by a lipid. The phosphate groups of the nucleotide are coordinated via two magnesium ions to the side-chain carboxyl groups of aspartates. Structure-function analysis, overview. Construction of the B3LYP/MM optimized structure corresponding to the transition state of the phosphoryl transfer step for the substrate-assisted mechanism obtained in the wild-type enzyme, and in the E526K mutant 759376
Show all pathways known for 2.7.1.29Display the word mapDisplay the reaction diagram Show all sequences 2.7.1.29more biological plausibility of virus-host associations, overview. Map of virus-host interactions generated by aligning spacers detected with reference-guided methods in metagenomes SS13, SS19, SS33, SS37, IC21, and Cahuil/C34 -, 759901
Results 1 - 6 of 6