ArticleApplied microbiology and biotechnology2008
Characterization of a modular enzyme of exo-1,5-alpha-L-arabinofuranosidase and arabinan binding module from Streptomyces avermitilis NBRC14893.
Article in Applied microbiology and biotechnology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.
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28 citing papers in PubMed, 62 citations in OpenAlex.
- Crystal structure of endo-β-1,6-galactanase from Streptomyces avermitilis.Acta crystallographica. Section D, Structural biology · 2026Article
- Characteristics and genome analysis of Enterobacter bugandensis C5-7 reveal its utilization value of maize growth promotion in saline-alkali land.World journal of microbiology & biotechnology · 2026Article
- Complementary GH54 and GH43 α-L-Arabinofuranosidases fromJournal of applied glycoscience · 2026Article
- Functional and structural characterization of AtAbf43C: an exo-1,5-α-L-arabinofuranosidase from Acetivibrio thermocellus DSM1313.The Biochemical journal · 2025Article
- Harnessing Xylanase Potential inJournal of fungi (Basel, Switzerland) · 2025Article
- Functional Characterization of Endo- and Exo-Hydrolase Genes in Arabinan Degradation Gene Cluster ofInternational journal of molecular sciences · 2024Article
- Two α-L-arabinofuranosidases from Bifidobacterium longum subsp. longum are involved in arabinoxylan utilization.Applied microbiology and biotechnology · 2022Article
- Characterization of a GH Family 43 β-Xylosidase Having a Novel Carbohydrate-binding Module fromJournal of applied glycoscience · 2022Article
- Arabinoxylo- and Arabino-Oligosaccharides-Specific α-L-Arabinofuranosidase GH51 Isozymes from the Amylolytic YeastJournal of microbiology and biotechnology · 2021Article
- Characterization of two extracellular arabinanases in Lactobacillus crispatus.Applied microbiology and biotechnology · 2020Article
- Molecular Characterization, Regioselective and Synergistic Action of First Recombinant Type III α-L-arabinofuranosidase of Family 43 Glycoside Hydrolase (PsGH43_12) from Pseudopedobacter saltans.Molecular biotechnology · 2020Article
- Article
- Two Novel α-l-Arabinofuranosidases fromApplied and environmental microbiology · 2019Article
- GH30 Glucuronoxylan-Specific Xylanase from Streptomyces turgidiscabies C56.Applied and environmental microbiology · 2018Article
- Characterisation of a Hydroxycinnamic Acid Esterase From theFrontiers in microbiology · 2018Article
- Comparative Genomics Reveals the Regulatory Complexity of Bifidobacterial Arabinose and Arabino-Oligosaccharide Utilization.Frontiers in microbiology · 2018Article
- Purification, Cloning, Functional Expression, Structure, and Characterization of a Thermostable β-Mannanase fromJournal of applied glycoscience · 2018Article
- Two Distinct α-l-Arabinofuranosidases in Caldicellulosiruptor Species Drive Degradation of Arabinose-Based Polysaccharides.Applied and environmental microbiology · 2017Article
- Crystal structure and characterization of the glycoside hydrolase family 62 α-L-arabinofuranosidase from Streptomyces coelicolor.The Journal of biological chemistry · 2014Article
- Overexpression, crystallization and preliminary X-ray crystallographic analysis of glucuronoxylan xylanohydrolase (Xyn30A) from Clostridium thermocellum.Acta crystallographica. Section F, Structural biology and crystallization communications · 2013Article
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4 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
A gene encoding an alpha-L-arabinofuranosidase, designated SaAraf43A, was cloned from Streptomyces avermitilis. The deduced amino acid sequence implies a modular structure consisting of an N-terminal glycoside hydrolase family 43 module and a C-terminal family 42 carbohydrate-binding module (CBM42). The recombinant enzyme showed optimal activity at pH 6.0 and 45 degrees C and was stable over the pH range of 5.0-6.5 at 30 degrees C. The enzyme hydrolyzed p-nitrophenol (PNP)-alpha-L-arabinofuranoside but did not hydrolyze PNP-alpha-L-arabinopyranoside, PNP-beta-D-xylopyranoside, or PNP-beta-D-galactopyranoside. Debranched 1,5-arabinan was hydrolyzed by the enzyme but arabinoxylan, arabinogalactan, gum arabic, and arabinan were not. Among the synthetic regioisomers of arabinofuranobiosides, only methyl 5-O-alpha-L-arabinofuranosyl-alpha-L-arabinofuranoside was hydrolyzed by the enzyme, while methyl 2-O-alpha-L-arabinofuranosyl-alpha-L-arabinofuranoside and methyl 3-O-alpha-L-arabinofuranosyl-alpha-L-arabinofuranoside were not. These data suggested that the enzyme only cleaves alpha-1,5-linked arabinofuranosyl linkages. The analysis of the hydrolysis product of arabinofuranopentaose suggested that the enzyme releases arabinose in exo-acting manner. These results indicate that the enzyme is definitely an exo-1,5-alpha-L-arabinofuranosidase. The C-terminal CBM42 did not show any affinity for arabinogalactan and debranched arabinan, although it bound arabinan and arabinoxylan, suggesting that the CBM42 bound to branched arabinofuranosyl residues. Removal of the module decreased the activity of the enzyme with regard to debranched arabinan. The CBM42 plays a role in enhancing the debranched arabinan hydrolytic action of the catalytic module in spite of its preference for binding arabinofuranosyl side chains.
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