4amx › Citations

Crystal structure of α-1,4-glucan lyase, a unique glycoside hydrolase family member with a novel catalytic mechanism.

Rozeboom HJ, Yu S, Madrid S, Kalk KH, Zhang R, Dijkstra BW
J Biol Chem 288 26764-74 (2013)
Related entries: 2x2h, 2x2i, 2x2j, 4amw

Cited: 12 times
EuropePMC logo PMID: 23902768

Abstract

α-1,4-Glucan lyase (EC 4.2.2.13) from the red seaweed Gracilariopsis lemaneiformis cleaves α-1,4-glucosidic linkages in glycogen, starch, and malto-oligosaccharides, yielding the keto-monosaccharide 1,5-anhydro-D-fructose. The enzyme belongs to glycoside hydrolase family 31 (GH31) but degrades starch via an elimination reaction instead of hydrolysis. The crystal structure shows that the enzyme, like GH31 hydrolases, contains a (β/α)8-barrel catalytic domain with B and B' subdomains, an N-terminal domain N, and the C-terminal domains C and D. The N-terminal domain N of the lyase was found to bind a trisaccharide. Complexes of the enzyme with acarbose and 1-dexoynojirimycin and two different covalent glycosyl-enzyme intermediates obtained with fluorinated sugar analogues show that, like GH31 hydrolases, the aspartic acid residues Asp(553) and Asp(665) are the catalytic nucleophile and acid, respectively. However, as a unique feature, the catalytic nucleophile is in a position to act also as a base that abstracts a proton from the C2 carbon atom of the covalently bound subsite -1 glucosyl residue, thus explaining the unique lyase activity of the enzyme. One Glu to Val mutation in the active site of the homologous α-glucosidase from Sulfolobus solfataricus resulted in a shift from hydrolytic to lyase activity, demonstrating that a subtle amino acid difference can promote lyase activity in a GH31 hydrolase.

Articles - 4amx mentioned but not cited (2)

  1. The carbohydrate-active enzymes database (CAZy) in 2013. Lombard V, Golaconda Ramulu H, Drula E, Coutinho PM, Henrissat B. Nucleic Acids Res 42 D490-5 (2014)
  2. Crystal structure of α-1,4-glucan lyase, a unique glycoside hydrolase family member with a novel catalytic mechanism. Rozeboom HJ, Yu S, Madrid S, Kalk KH, Zhang R, Dijkstra BW. J Biol Chem 288 26764-26774 (2013)


Reviews citing this publication (2)

  1. α-Glucosidases and α-1,4-glucan lyases: structures, functions, and physiological actions. Okuyama M, Saburi W, Mori H, Kimura A. Cell Mol Life Sci 73 2727-2751 (2016)
  2. Hypothesis: A Novel Neuroprotective Role for Glucose-6-phosphatase (G6PC3) in Brain-To Maintain Energy-Dependent Functions Including Cognitive Processes. Dienel GA. Neurochem Res 45 2529-2552 (2020)

Articles citing this publication (8)

  1. Structure of human lysosomal acid α-glucosidase-a guide for the treatment of Pompe disease. Roig-Zamboni V, Cobucci-Ponzano B, Iacono R, Ferrara MC, Germany S, Bourne Y, Parenti G, Moracci M, Sulzenbacher G. Nat Commun 8 1111 (2017)
  2. Structural insight into how Streptomyces coelicolor maltosyl transferase GlgE binds α-maltose 1-phosphate and forms a maltosyl-enzyme intermediate. Syson K, Stevenson CE, Rashid AM, Saalbach G, Tang M, Tuukkanen A, Svergun DI, Withers SG, Lawson DM, Bornemann S. Biochemistry 53 2494-2504 (2014)
  3. Metal Dependence of the Xylose Isomerase from Piromyces sp. E2 Explored by Activity Profiling and Protein Crystallography. Lee M, Rozeboom HJ, de Waal PP, de Jong RM, Dudek HM, Janssen DB. Biochemistry 56 5991-6005 (2017)
  4. A glycoside hydrolase family 31 dextranase with high transglucosylation activity from Flavobacterium johnsoniae. Gozu Y, Ishizaki Y, Hosoyama Y, Miyazaki T, Nishikawa A, Tonozuka T. Biosci Biotechnol Biochem 80 1562-1567 (2016)
  5. A glycan FRET assay for detection and characterization of catalytic antibodies to the Cryptococcus neoformans capsule. Crawford CJ, Wear MP, Smith DFQ, d'Errico C, McConnell SA, Casadevall A, Oscarson S. Proc Natl Acad Sci U S A 118 e2016198118 (2021)
  6. Structural basis of the strict specificity of a bacterial GH31 α-1,3-glucosidase for nigerooligosaccharides. Ikegaya M, Moriya T, Adachi N, Kawasaki M, Park EY, Miyazaki T. J Biol Chem 298 101827 (2022)
  7. A Full QM Computational Study of the Catalytic Mechanism of α-1,4-Glucan Lyases. Campesato L, Marforio TD, Giacinto P, Calvaresi M, Bottoni A. Chemphyschem 19 1514-1521 (2018)
  8. A subfamily classification to choreograph the diverse activities within glycoside hydrolase family 31. Arumapperuma T, Li J, Hornung B, Soler NM, Goddard-Borger ED, Terrapon N, Williams SJ. J Biol Chem 299 103038 (2023)


Quick links