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

Lee, Sun Bok; Lee, Shin Youp; Lim, Hyun Seung

doi:10.1007/s12257-015-0520-3

Cited by 2 publications

(1 citation statement)

References 26 publications

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“…In addition to the catalytic residues, the conformational changes of non-catalytic residues in the substrate channel upon the binding of NAD + also induce the connection of two separate channels in the betaine aldehyde dehydrogenase from Staphylococcus aureus (21). For AHGDs, only the structure of the apo Patl_2553 was deposited in the Protein Data Bank (PDB) by the New York SGX Research Center for Structural Genomics team, and this structure was preliminarily analyzed by Sun et al (26).…”

Section: Introductionmentioning

confidence: 99%

3,6-Anhydro-L-Galactose Dehydrogenase VvAHGD is a Member of a New Aldehyde Dehydrogenase Family and Catalyzes by a Novel Mechanism with Conformational Switch of Two Catalytic Residues Cysteine 282 and Glutamate 248

Wang

Zhang

et al. 2020

Journal of Molecular Biology

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Section: Introductionmentioning

confidence: 99%

3,6-Anhydro-L-Galactose Dehydrogenase VvAHGD is a Member of a New Aldehyde Dehydrogenase Family and Catalyzes by a Novel Mechanism with Conformational Switch of Two Catalytic Residues Cysteine 282 and Glutamate 248

Wang

Zhang

et al. 2020

Journal of Molecular Biology

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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

Cited by 2 publications

References 26 publications

3,6-Anhydro-L-Galactose Dehydrogenase VvAHGD is a Member of a New Aldehyde Dehydrogenase Family and Catalyzes by a Novel Mechanism with Conformational Switch of Two Catalytic Residues Cysteine 282 and Glutamate 248

3,6-Anhydro-L-Galactose Dehydrogenase VvAHGD is a Member of a New Aldehyde Dehydrogenase Family and Catalyzes by a Novel Mechanism with Conformational Switch of Two Catalytic Residues Cysteine 282 and Glutamate 248

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

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