Biochemistry of coenzyme B12-dependent glycerol and diol dehydratases and organization of the encoding genes

Daniel, Rolf

doi:10.1016/s0168-6445(98)00021-7

Cited by 55 publications

(96 citation statements)

References 43 publications

(106 reference statements)

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“…Transmembrane segments (TMSs) were predicted using the TMpred program (www.ch.embnet.org/software/TMPRED_form.html). 2 A. Mironov, unpublished results. …”

Section: Methodsmentioning

confidence: 71%

“…Among the most prominent vitamin B 12 -dependent enzymes in bacteria and archaea are the methionine synthase isozyme MetH from enteric bacteria; the ribonucleotide reductase isozyme NrdJ from deeply rooted eubacteria and archaea; diol dehydratases and ethanolamine ammonia lyase from enteric bacteria involved in anaerobic glycerol, 1,2-propanediol, and ethanolamine fermentation; glutamate and methylmalonyl-CoA mutases from clostridia and streptomycetes; and various CBL-dependent methyltransferases from methane-producing archaea (1)(2)(3)(4)(5).…”

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confidence: 99%

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Comparative Genomics of the Vitamin B12 Metabolism and Regulation in Prokaryotes

Rodionov

Vitreschak

Mironov

et al. 2003

Journal of Biological Chemistry

407

426

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Using comparative analysis of genes, operons, and regulatory elements, we describe the cobalamin (vitamin B 12 ) biosynthetic pathway in available prokaryotic genomes. Here we found a highly conserved RNA secondary structure, the regulatory B12 element, which is widely distributed in the upstream regions of cobalamin biosynthetic/transport genes in eubacteria. In addition, the binding signal (CBL-box) for a hypothetical B 12 regulator was identified in some archaea. A search for B12 elements and CBL-boxes and positional analysis identified a large number of new candidate B 12 -regulated genes in various prokaryotes. Among newly assigned functions associated with the cobalamin biosynthesis, there are several new types of cobalt transporters, ChlI and ChlD subunits of the CobN-dependent cobaltochelatase complex, cobalt reductase BluB, adenosyltransferase PduO, several new proteins linked to the lower ligand assembly pathway, L-threonine kinase PduX, and a large number of other hypothetical proteins. Most missing genes detected within the cobalamin biosynthetic pathways of various bacteria were identified as nonorthologous substitutes. The variable parts of the cobalamin metabolism appear to be the cobalt transport and insertion, the CobG/CbiG-and CobF/CbiD-catalyzed reactions, and the lower ligand synthesis pathway. The most interesting result of analysis of B12 elements is that B 12 -independent isozymes of the methionine synthase and ribonucleotide reductase are regulated by B12 elements in bacteria that have both B 12 -dependent and B 12 -independent isozymes. Moreover, B 12 regulons of various bacteria are thought to include enzymes from known B 12 -dependent or alternative pathways. Cobalamin (CBL),1 along with chlorophyll, heme, siroheme, and coenzyme F 430 , constitute a class of the most structurally complex cofactors synthesized by bacteria. The distinctive feature of these cofactors is their tetrapyrrole-derived framework with a centrally chelated metal ion (cobalt, magnesium, iron, or nickel). Methylcobalamin and Ado-CBL, two derivatives of vitamin B 12 (cyanocobalamin) with different upper axial ligands, are essential cofactors for several important enzymes that catalyze a variety of transmethylation and rearrangement reactions. Among the most prominent vitamin B 12 -dependent enzymes in bacteria and archaea are the methionine synthase isozyme MetH from enteric bacteria; the ribonucleotide reductase isozyme NrdJ from deeply rooted eubacteria and archaea; diol dehydratases and ethanolamine ammonia lyase from enteric bacteria involved in anaerobic glycerol, 1,2-propanediol, and ethanolamine fermentation; glutamate and methylmalonyl-CoA mutases from clostridia and streptomycetes; and various CBL-dependent methyltransferases from methane-producing archaea (1-5).Most prokaryotic organisms as well as animals (including humans) and protists have enzymes that require CBL as cofactor, whereas plants and fungi are thought not to use it. Among the CBL-utilizing organisms, only some bacterial and archaeal species ...

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“…Transmembrane segments (TMSs) were predicted using the TMpred program (www.ch.embnet.org/software/TMPRED_form.html). 2 A. Mironov, unpublished results. …”

Section: Methodsmentioning

confidence: 71%

mentioning

confidence: 99%

Comparative Genomics of the Vitamin B12 Metabolism and Regulation in Prokaryotes

Rodionov

Vitreschak

Mironov

et al. 2003

Journal of Biological Chemistry

407

426

View full text Add to dashboard Cite

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“…This broadspectrum antimicrobial compound is a mixture of monomeric, hydrated monomeric and cyclic dimeric forms of 3-hydroxypropionaldehyde (3-HPA) (Talarico & Dobrogosz, 1989). The synthesis of reuterin is mediated by glycerol dehydratase (EC 4.2.1.30), a vitamin B 12 -dependent enzyme, which is involved in catalysing the conversion of glycerol to 3-HPA (Daniel et al, 1998).…”

Section: Introductionmentioning

confidence: 99%

The complete coenzyme B12 biosynthesis gene cluster of Lactobacillus reuteri CRL1098

et al. 2008

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“…Finally, one of the key limitations of the application of this biological process to industry is that it requires the coenzyme B 12 -dependent glycerol dehydratase, necessitating the addition of large amounts of a high-cost molecule, vitamin B 12 , to the culture medium. Hence, to establish an ideal bioprocess for 1,3-PD production, at least three challenges need to addressed: (i) the effect of accumulated 3-HPA on glycerol dehydratase activity; (ii) the inactivation of glycerol dehydratase by glycerol (8); (iii) the expense of coenzyme vitamin B 12 in fermentation.…”

mentioning

confidence: 99%

Microbial Conversion of Glycerol to 1,3-Propanediol by an Engineered Strain of Escherichia coli

Tang

Tan

Hong

et al. 2009

Appl Environ Microbiol

141

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In an effort to improve industrial production of 1,3-propanediol (1,3-PD), we engineered a novel polycistronic operon under the control of the temperature-sensitive lambda phage P L P R promoter regulated by the cIts857 repressor and expressed it in Escherichia coli K-12 ER2925. The genes for the production of 1,3-PD in Clostridium butyricum, dhaB1 and dhaB2, which encode the vitamin B 12 -independent glycerol dehydratase DhaB1 and its activating factor, DhaB2, respectively, were tandemly arrayed with the E. coli yqhD gene, which encodes the 1,3-propanediol oxidoreductase isoenzyme YqhD, an NADP-dependent dehydrogenase that can directly convert glycerol to 1,3-PD. The microbial conversion of 1,3-PD from glycerol by this recombinant E. coli strain was studied in a two-stage fermentation process. During the first stage, a novel high-cell-density fermentation step, there was significant cell growth and the majority of the metabolites produced were organic acids, mainly acetate. During the second stage, glycerol from the fresh medium was rapidly converted to 1,3-PD following a temperature shift from 30°C to 42°C. The by-products were mainly pyruvate and acetate. During this two-stage process, the overall 1,3-PD yield and productivity reached 104.4 g/liter and 2.61 g/liter/h, respectively, and the conversion rate of glycerol to 1,3-PD reached 90.2% (g/g). To our knowledge, this is the highest reported yield and productivity efficiency of 1,3-PD with glycerol as the sole source of carbon. Furthermore, the overall fermentation time was only 40 h, shorter than that of any other reports.

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Biochemistry of coenzyme B12-dependent glycerol and diol dehydratases and organization of the encoding genes

Cited by 55 publications

References 43 publications

Comparative Genomics of the Vitamin B12 Metabolism and Regulation in Prokaryotes

Comparative Genomics of the Vitamin B12 Metabolism and Regulation in Prokaryotes

The complete coenzyme B12 biosynthesis gene cluster of Lactobacillus reuteri CRL1098

Microbial Conversion of Glycerol to 1,3-Propanediol by an Engineered Strain of Escherichia coli

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