This view shows enzymes only for those organisms listed below, in the list of taxa known to possess the pathway. If an enzyme name is shown in bold, there is experimental evidence for this enzymatic activity.
|Superclasses:||Biosynthesis → Secondary Metabolites Biosynthesis → Alcohols Biosynthesis|
Some taxa known to possess this pathway include : Clostridium pasteurianum
Expected Taxonomic Range: Bacteria
The production of biofuels from renewable feedstock is a growing field, in the face of dwindling supplies and the cost of petroleum-based fuels. The primary alcohol butanol is an excellent example of a good biofuel, and is produced by several species of Clostridium. Butanol is produced by Clostridium acetobutylicum and Clostridium pasteurianum by the process of acetone-butanol-ethanol (ABE) fermentation. However, this system is hampered by productivity limitations. To circumvent these issues Clostridium pasteurianum was chemically mutated to produce copious amounts of butanol using glycerol as the sole carbon source [Malaviya12]. Glycerol is a good feedstock for butanol production because it is inexpensive and readily available, being a byproduct of biodiesel production.
About this Pathway
The butanol biosynthesis pathway from glycerol, depicted here is a naturally occurring one in Clostridium pasteurianum, albeit a system with a low yield of butanol due to the limitations of the naturally occurring ABE fermentation mechanism. Using the same pathway, Clostridium pasteurianum was chemically mutated using N-methyl-N'-nitro-N-nitrosoguanidine (NTG) to become a hyper producer of butanol.
Subpathways: glycerol degradation II
Malaviya12: Malaviya A, Jang YS, Lee SY (2012). "Continuous butanol production with reduced byproducts formation from glycerol by a hyper producing mutant of Clostridium pasteurianum." Appl Microbiol Biotechnol 93(4);1485-94. PMID: 22052388
Abbe83: Abbe K, Takahashi S, Yamada T (1983). "Purification and properties of pyruvate kinase from Streptococcus sanguis and activator specificity of pyruvate kinase from oral streptococci." Infect Immun 39(3);1007-14. PMID: 6840832
Alber06: Alber BE, Spanheimer R, Ebenau-Jehle C, Fuchs G (2006). "Study of an alternate glyoxylate cycle for acetate assimilation by Rhodobacter sphaeroides." Mol Microbiol 61(2);297-309. PMID: 16856937
Alvarez98: Alvarez M, Zeelen JP, Mainfroid V, Rentier-Delrue F, Martial JA, Wyns L, Wierenga RK, Maes D (1998). "Triose-phosphate isomerase (TIM) of the psychrophilic bacterium Vibrio marinus. Kinetic and structural properties." J Biol Chem 273(4);2199-206. PMID: 9442062
Ashizawa91: Ashizawa K, McPhie P, Lin KH, Cheng SY (1991). "An in vitro novel mechanism of regulating the activity of pyruvate kinase M2 by thyroid hormone and fructose 1, 6-bisphosphate." Biochemistry 30(29);7105-11. PMID: 1854723
Beaucamp97: Beaucamp N, Hofmann A, Kellerer B, Jaenicke R (1997). "Dissection of the gene of the bifunctional PGK-TIM fusion protein from the hyperthermophilic bacterium Thermotoga maritima: design and characterization of the separate triosephosphate isomerase." Protein Sci 1997;6(10);2159-65. PMID: 9336838
Beaucamp97a: Beaucamp N, Schurig H, Jaenicke R (1997). "The PGK-TIM fusion protein from Thermotoga maritima and its constituent parts are intrinsically stable and fold independently." Biol Chem 1997;378(7);679-85. PMID: 9278147
Beh93: Beh M, Strauss G, Huber R, Stetter K-O, Fuchs G (1993). "Enzymes of the reductive citric acid cycle in the autotrophic eubacterium Aquifex pyrophilus and in the archaebacterium Thermoproteus neutrophilus." Arch Microbiol 160: 306-311.
Blamey93: Blamey JM, Adams MW (1993). "Purification and characterization of pyruvate ferredoxin oxidoreductase from the hyperthermophilic archaeon Pyrococcus furiosus." Biochim Biophys Acta 1161(1);19-27. PMID: 8380721
Blamey94: Blamey JM, Adams MW (1994). "Characterization of an ancestral type of pyruvate ferredoxin oxidoreductase from the hyperthermophilic bacterium, Thermotoga maritima." Biochemistry 1994;33(4);1000-7. PMID: 8305426
Blaschkowski82: Blaschkowski HP, Neuer G, Ludwig-Festl M, Knappe J (1982). "Routes of flavodoxin and ferredoxin reduction in Escherichia coli. CoA-acylating pyruvate: flavodoxin and NADPH: flavodoxin oxidoreductases participating in the activation of pyruvate formate-lyase." Eur J Biochem 123(3);563-9. PMID: 7042345
Boiteux83: Boiteux A, Markus M, Plesser T, Hess B, Malcovati M (1983). "Analysis of progress curves. Interaction of pyruvate kinase from Escherichia coli with fructose 1,6-bisphosphate and calcium ions." Biochem J 1983;211(3);631-40. PMID: 6349612
Botha86: Botha FC, Dennis DT (1986). "Isozymes of phosphoglyceromutase from the developing endosperm of Ricinus communis: isolation and kinetic properties." Arch Biochem Biophys 245(1);96-103. PMID: 3004361
Branlant85: Branlant G, Branlant C (1985). "Nucleotide sequence of the Escherichia coli gap gene. Different evolutionary behavior of the NAD+-binding domain and of the catalytic domain of D-glyceraldehyde-3-phosphate dehydrogenase." Eur J Biochem 1985;150(1);61-6. PMID: 2990926
Branny98: Branny P, de la Torre F, Garel JR (1998). "An operon encoding three glycolytic enzymes in Lactobacillus delbrueckii subsp. bulgaricus: glyceraldehyde-3-phosphate dehydrogenase, phosphoglycerate kinase and triosephosphate isomerase." Microbiology 144 ( Pt 4);905-14. PMID: 9579064
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