Identification and characterization of 3,6-anhydro-L-galactonate cycloisomerase belonging to theenolase superfamily

Cho, Sun Ja; Kim, Jeong Ah; Lee, Sun Bok

doi:10.1007/s12257-015-0359-7

Cited by 5 publications

(9 citation statements)

References 29 publications

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“…Recently, the 3,6-anhydro-L-galactose dehydrogenase (LAnGDH) [2] and 3,6-anhydro-L-galactonate cycloisomerase (L-AnGACI) [3] from Postechiella marina M091 have been characterized. P. marina M091, which was isolated from a seawater sample obtained at Damupo beach in Pohang, Korea, is a novel agar-degrading microorganism belonging to a new genus within the family Flavobacteriaceae [9].…”

Section: Previous Studies On L-angdh and L-angacimentioning

confidence: 99%

“…L-AnGACI is an enzyme catalyzing the second step of the L-AnG pathway and catalyzes the cycloisomerization of a cyclic compound (L-AnGA) into an acyclic isomer (LKDGal) [1,3]. The conversion of L-AnGA to L-KDGal, was confirmed by the L-KDGal aldolase reaction and the LC-MS analysis of the aldolase reaction products.…”

Section: Previous Studies On L-angdh and L-angacimentioning

confidence: 99%

“…The conversion of L-AnGA to L-KDGal, was confirmed by the L-KDGal aldolase reaction and the LC-MS analysis of the aldolase reaction products. The fungal L-KDGal aldolase (An02g07720) specifically degraded L-KDGal to pyruvate and L-glyceraldehyde and showed no activity toward D-KDGal [1,3]. A proposed reaction mechanism for cycloisomerization of L-AnGA to L-KDGal implies that the L-configuration does not change during the reaction [3].…”

Section: Previous Studies On L-angdh and L-angacimentioning

confidence: 99%

“…1A). They also have conducted in-depth studies on 3,6-anhydro-L-galactose dehydrogenase (LAnGDH) [2] and 3,6-anhydro-L-galactonate cycloisomerase (L-AnGACI) [3], which are the first and the second step of the L-AnG pathway of three agar-degrading microorganisms. The metabolic pathway of L-AnG in another marine microorganism, Vibrio sp.…”

Section: Introductionmentioning

confidence: 99%

“…On the contrary, Lee et al's data showed that the product of the reaction catalyzed by L-AnGACI is 2-keto-3-deoxy-L-galactonate (L-KDGal). Formation of L-KDGal from 3,6-anhydro-L-galactonate was verified using fungal L-KDGal aldolase (An02g07720), which specifically degrades L-KDGal to pyruvate and L-glyceraldehyde [1,3]. This aldolase shows no activity toward D-KDGal [3].…”

Section: Introductionmentioning

confidence: 99%

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Unusual metabolism of 3,6-anhydro-L-galactose in Vibrio sp. EJY3 and in E. coli containing two Vibrio sp. EJY3 genes

Lee

2015

Biotechnol Bioproc E

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Recently, Yun et al. [Envron. Microbiol. 17: 1677-1688] proposed a metabolic pathway of 3,6-anhydro-L-galactose (L-AnG) in Vibrio sp. EJY3. The sequence of Yun's pathway is 3,6-anhydro-L-galactose → 3,6-anhydro-galactonate → 2-keto-3-deoxy-galactonate → DeLey-Doudoroff pathway. This pathway differs significantly from one that has been established by Lee et al. [Biotechnol. Bioproc. Eng. 19: 866-878 (2014)], and which has been detected in agar-degrading bacteria such as Postechiella marina M091, Pseudoalteromonas atlantica T6c, and Streptomyces coelicolor A3(2). The sequence of Lee's pathway is 3,6-anhydro-L-galactose → 3,6-anhydro-Lgalactonate → 2-keto-3-deoxy-L-galactonate → 2,5-diketo-3-deoxy-L-galactonate → 2-keto-3-deoxy-D-gluconate → 2-keto-3-deoxy-6-phospho-D-gluconate → pyruvate + Dglyceraldehyde-3-phosphate. Because Yun's L-AnG pathway is connected to the DeLey-Doudoroff pathway and 2-keto-3-deoxy-D-galactonate (D-KDGal) is an intermediate in the DeLey-Doudoroff pathway, the 2-keto-3-deoxy-galactonate in the Yun's pathway must be D-KDGal. On the contrary, Lee et al. showed that the product of the reaction catalyzed by the second-step enzyme is 2-keto-3-deoxy-L-galactonate (L-KDGal). The E. coli genome contains the genes that enable conversion of D-KDGal to glycolysis intermediates via the DeLey-Doudoroff pathway. However, if the reaction product of the second-step enzyme is L-KDGal, additional genes are required for the conversion of L-KDGal to glycolysis intermediates. Here I argue that the validity of the following claims by Yun et al. is very questionable: (1) the formation of D-KDGal during the metabolism of L-AnG in Vibrio sp. EJY3 and (2) the production of ethanol from L-AnG using the DeLey-Doudoroff pathway in E. coli.

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Section: Previous Studies On L-angdh and L-angacimentioning

confidence: 99%

Section: Previous Studies On L-angdh and L-angacimentioning

confidence: 99%

Section: Previous Studies On L-angdh and L-angacimentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Unusual metabolism of 3,6-anhydro-L-galactose in Vibrio sp. EJY3 and in E. coli containing two Vibrio sp. EJY3 genes

Lee

2015

Biotechnol Bioproc E

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Metabolic pathway of 3,6-anhydro-D-galactose in carrageenan-degrading microorganisms

Lee

Kim

Lim

2016

Appl Microbiol Biotechnol

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Complete hydrolysis of κ-carrageenan produces two sugars, D-galactose and 3,6-anhydro-D-galactose (D-AnG). At present, however, we do not know how carrageenan-degrading microorganisms metabolize D-AnG. In this study, we investigated the metabolic pathway of D-AnG degradation by comparative genomic analysis of Cellulophaga lytica LIM-21, Pseudoalteromonas atlantica T6c, and Epulopiscium sp. N.t. morphotype B, which represent the classes Flavobacteria, Gammaproteobacteria, and Clostridia, respectively. In this bioinformatic analysis, we found candidate common genes that were believed to be involved in D-AnG metabolism. We then experimentally confirmed the enzymatic function of each gene product in the D-AnG cluster. In all three microorganisms, D-AnG metabolizing genes were clustered and organized in operon-like arrangements, which we named as the dan operon (3,6-d-anhydro-galactose). Combining bioinformatic analysis and experimental data, we showed that D-AnG is metabolized to pyruvate and D-glyceraldehyde-3-phosphate via four enzyme-catalyzed reactions in the following route: 3,6-anhydro-D-galactose → 3,6-anhydro-D-galactonate → 2-keto-3-deoxy-D-galactonate (D-KDGal) → 2-keto-3-deoxy-6-phospho-D-galactonate → pyruvate + D-glyceraldehyde-3-phosphate. The pathway of D-AnG degradation is composed of two parts: transformation of D-AnG to D-KDGal using two D-AnG specific enzymes and breakdown of D-KDGal to two glycolysis intermediates using two DeLey-Doudoroff pathway enzymes. To our knowledge, this is the first report on the metabolic pathway of D-AnG degradation.

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Aldehydic nature and conformation of 3,6-anhydro-L-galactose monomer

Lee

Lim

2015

Biotechnol Bioproc E

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Identification and characterization of 3,6-anhydro-L-galactonate cycloisomerase belonging to theenolase superfamily

Cited by 5 publications

References 29 publications

Unusual metabolism of 3,6-anhydro-L-galactose in Vibrio sp. EJY3 and in E. coli containing two Vibrio sp. EJY3 genes

Unusual metabolism of 3,6-anhydro-L-galactose in Vibrio sp. EJY3 and in E. coli containing two Vibrio sp. EJY3 genes

Metabolic pathway of 3,6-anhydro-D-galactose in carrageenan-degrading microorganisms

Aldehydic nature and conformation of 3,6-anhydro-L-galactose monomer

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