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:||Degradation/Utilization/Assimilation → Carboxylates Degradation → Sugar Acids Degradation → D-Glucarate Degradation|
|Degradation/Utilization/Assimilation → Secondary Metabolites Degradation → Sugar Derivatives Degradation → Sugar Acids Degradation → D-Glucarate Degradation|
Some taxa known to possess this pathway include : Acinetobacter sp. ADP1 , Agrobacterium fabrum C58 , Agrobacterium tumefaciens , Delftia acidovorans , Pseudomonas putida , Pseudomonas sp. , Pseudomonas syringae
Expected Taxonomic Range: Bacteria
D-glucarate is a naturally occurring dicarboxylate that can be used by some species of bacteria. Enterobacteria such as Escherichia coli and Klebsiella aerogenes utilize it by a different pathway than the one shown here (see pathway D-glucarate degradation I). Both pathways start with a dehydratase that produces 5-dehydro-4-deoxy-D-glucarate [Jeffcoat69]. Some bacteria possess an inducible uronate dehydrogenase that catalyzes the conversion of D-glucuronate to D-glucarate as shown in the pathway link. Although the genes in the pathway shown here remain uncharacterized in most of the organisms listed, more recent work in Acinetobacter sp. ADP1 (previously known as Acinetobacter baylyi ADP1) identified the genes involved in this pathway and pathway D-galactarate degradation II, including a D-glucararte/D-galactarate permease [Aghaie08].
About This Pathway
In Acinetobacter sp. ADP1 genes encoding enzymes for the degradation of D-glucarate and galactarate were identified by mutant analysis and complementation studies and the recombinant gene products were characterized. Intermediates in the pathway were identified by LC/MS [Aghaie08]. Genes included a D-glucarate/D-galactarate permease; separate, specific dehydratases for D-glucarate and galactarate; a 5-dehydro-4-deoxy-D-gluccarate dehydratase; and a 2-oxoglutarate semialdehyde dehydrogenase (also see pathway D-galactarate degradation II). The 2-oxoglutarate (α-ketoglutarate) produced in the pathway can be metabolized in the TCA cycle I (prokaryotic) as shown in the pathway link, or used in many other pathways.
Variants: D-glucarate degradation I
Aghaie08: Aghaie A, Lechaplais C, Sirven P, Tricot S, Besnard-Gonnet M, Muselet D, de Berardinis V, Kreimeyer A, Gyapay G, Salanoubat M, Perret A (2008). "New insights into the alternative D-glucarate degradation pathway." J Biol Chem 283(23);15638-46. PMID: 18364348
Andberg12: Andberg M, Maaheimo H, Boer H, Penttila M, Koivula A, Richard P (2012). "Characterization of a novel Agrobacterium tumefaciens galactarolactone cycloisomerase enzyme for direct conversion of D-galactarolactone to 3-deoxy-2-keto-L-threo-hexarate." J Biol Chem 287(21);17662-71. PMID: 22493433
Brouns06: Brouns SJ, Walther J, Snijders AP, van de Werken HJ, Willemen HL, Worm P, de Vos MG, Andersson A, Lundgren M, Mazon HF, van den Heuvel RH, Nilsson P, Salmon L, de Vos WM, Wright PC, Bernander R, van der Oost J (2006). "Identification of the missing links in prokaryotic pentose oxidation pathways: evidence for enzyme recruitment." J Biol Chem 281(37);27378-88. PMID: 16849334
Gulick00: Gulick AM, Hubbard BK, Gerlt JA, Rayment I (2000). "Evolution of enzymatic activities in the enolase superfamily: crystallographic and mutagenesis studies of the reaction catalyzed by D-glucarate dehydratase from Escherichia coli." Biochemistry 2000;39(16);4590-602. PMID: 10769114
Gulick01: Gulick AM, Hubbard BK, Gerlt JA, Rayment I (2001). "Evolution of enzymatic activities in the enolase superfamily: identification of the general acid catalyst in the active site of D-glucarate dehydratase from Escherichia coli." Biochemistry 40(34);10054-62. PMID: 11513584
Gulick98: Gulick AM, Palmer DR, Babbitt PC, Gerlt JA, Rayment I (1998). "Evolution of enzymatic activities in the enolase superfamily: crystal structure of (D)-glucarate dehydratase from Pseudomonas putida." Biochemistry 37(41);14358-68. PMID: 9772161
Hubbard98: Hubbard BK, Koch M, Palmer DR, Babbitt PC, Gerlt JA (1998). "Evolution of enzymatic activities in the enolase superfamily: characterization of the (D)-glucarate/galactarate catabolic pathway in Escherichia coli." Biochemistry 1998;37(41);14369-75. PMID: 9772162
Johnsen09: Johnsen U, Dambeck M, Zaiss H, Fuhrer T, Soppa J, Sauer U, Schonheit P (2009). "D-xylose degradation pathway in the halophilic archaeon Haloferax volcanii." J Biol Chem 284(40);27290-303. PMID: 19584053
Palmer96: Palmer D.R.J., Gerlt J.A. (1996). "Evolution of enzymatic activities: Multiple pathways for generating and partitioning a common enolic intermediate by glucarate dehydratase from Pseudomonas putida." J. Am. Chem. Soc. 118, 10323-10324.
Palmer98: Palmer DR, Hubbard BK, Gerlt JA (1998). "Evolution of enzymatic activities in the enolase superfamily: partitioning of reactive intermediates by (D)-glucarate dehydratase from Pseudomonas putida." Biochemistry 37(41);14350-7. PMID: 9772160
Watanabe12: Watanabe S, Morimoto D, Fukumori F, Shinomiya H, Nishiwaki H, Kawano-Kawada M, Sasai Y, Tozawa Y, Watanabe Y (2012). "Identification and characterization of D-hydroxyproline dehydrogenase and Delta1-pyrroline-4-hydroxy-2-carboxylate deaminase involved in novel L-hydroxyproline metabolism of bacteria: metabolic convergent evolution." J Biol Chem 287(39);32674-88. PMID: 22833679
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