The pathway starts with the methylation to malonyl-ACP methyl ester, followed by the fatty acid chain elongation cycle to form pimeloyl-ACP methyl ester, which is then demethylated to form pimeloyl-ACP [MD:].
AB - Biotin is an enzyme cofactor indispensable to metabolic fixation of carbon dioxide in all three domains of life. Although the catalytic and physiological roles of biotin have been well characterized, the biosynthesis of biotin remains to be fully elucidated. Studies in microbes suggest a two-stage biosynthetic pathway in which a pimelate moiety is synthesized and used to begin assembly of the biotin bicyclic ring structure. The enzymes involved in the bicyclic ring assembly have been studied extensively. In contrast the synthesis of pimelate, a seven carbon α,ω-dicarboxylate, has long been an enigma. Support for two different routes of pimelate synthesis has recently been obtained in Escherichia coli and Bacillus subtilis. The E. coli BioC-BioH pathway employs a methylation and demethylation strategy to allow elongation of a temporarily disguised malonate moiety to a pimelate moiety by the fatty acid synthetic enzymes whereas the B. subtilis BioI-BioW pathway utilizes oxidative cleavage of fatty acyl chains. Both pathways produce the pimelate thioester precursor essential for the first step in assembly of the fused rings of biotin. The enzymatic mechanisms and biochemical strategies of these pimelate synthesis models will be discussed in this review.
QIAGEN - GeneGlobe Pathways - Biotin Biosynthesis in …
To find the pathway link for 'Lysine biosynthesis', scroll down on the browser to the group of pathways called 'amino acid metabolism' and click on the link.
role for the biotin biosynthesis in ..
Ph.D. in Biochemistry, Fall 2013
Thesis: Characterization of acyl-ACP thioesterases for the purpose of diversifying fatty acid synthesis pathway
of biotin biosynthesis in the ..
This sheet lists compound entry number for L-lysine (note that D-lysine has a different entry, of course), common name(s), formula, structure, all pathway maps that contain L-lysine as metabolite (5 maps for L-lysine including synthesis and degradation, biotin metabolism, alkaloid biosynthesis II, and Aminoacyl-tRNA biosynthesis), and finally a list of all known enzymes that use L-lysine as a substrate.
KEGG PATHWAY: Biotin metabolism - Reference pathway
Ph.D. in Biochemistry, Fall 2012
Thesis: Chemical characterization of hydrocarbons and transcriptome profiling to elucidate pathway(s) of hydrocarbon biosynthesis in maize, pea, Botryococcus braunii and Emiliania huxleyi.
Biotin biosynthesis, transport and utilization in ..
AB - In most bacteria the last step in synthesis of the pimelate moiety of biotin is cleavage of the ester bond of pimeloyl-acyl carrier protein (ACP) methyl ester. The paradigm cleavage enzyme is Escherichia coli BioH which together with the BioC methyltransferase allows synthesis of the pimelate moiety by a modified fatty acid biosynthetic pathway. Analyses of the extant bacterial genomes showed that bioH is absent from many bioC-containing bacteria and is replaced by other genes. Helicobacter pylori lacks a gene encoding a homologue of the known pimeloyl-ACP methyl ester cleavage enzymes suggesting that it encodes a novel enzyme that cleaves this intermediate. We isolated the H. pylori gene encoding this enzyme, bioV, by complementation of an E. coli bioH deletion strain. Purified BioV cleaved the physiological substrate, pimeloyl-ACP methyl ester to pimeloyl-ACP by use of a catalytic triad, each member of which was essential for activity. The role of BioV in biotin biosynthesis was demonstrated using a reconstituted in vitro desthiobiotin synthesis system. BioV homologues seem the sole pimeloyl-ACP methyl ester esterase present in the Helicobacter species and their occurrence only in H. pylori and close relatives provide a target for development of drugs to specifically treat Helicobacter infections.