ArticleApplied and environmental microbiology2002
Identification and characterization of the gene cluster involved in chitin degradation in a marine bacterium, Alteromonas sp. strain O-7.
Article in Applied and environmental microbiology, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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21 citing papers in PubMed, 46 citations in OpenAlex.
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- Studies on insect virus-producing proteins as potential synergists for microbial insecticides: status and prospects.Virus genes · 2025Review
- Diversity and Potential Metabolic Characteristics of Culturable Copiotrophic Bacteria That Can Grow on Low-Nutrient Medium in Zhenbei Seamount in the South China Sea.Microbial ecology · 2024Article
- A pathway for chitin oxidation in marine bacteria.Nature communications · 2022Article
- Marine ChitinolyticmSystems · 2019Article
- 16S rRNA gene metabarcoding and TEM reveals different ecological strategies within the genus Neogloboquadrina (planktonic foraminifer).PloS one · 2018Article
- Biological Potential of Chitinolytic Marine Bacteria.Marine drugs · 2016Article
- Microdiversity of extracellular enzyme genes among sequenced prokaryotic genomes.The ISME journal · 2013Article
- Analysis of EpapGV gp37 gene reveals a close relationship between granulovirus and entomopoxvirus.Virus genes · 2012Article
- Aeromonas caviae CB101 contains four chitinases encoded by a single gene chi1.Molecular biotechnology · 2010Article
- The effects of the surface-exposed residues on the binding and hydrolytic activities of Vibrio carchariae chitinase A.BMC biochemistry · 2008Article
- Chitinase gene diversity at a deep sea station of the east Pacific nodule province.Extremophiles : life under extreme conditions · 2007Article
- Spindles of an entomopoxvirus facilitate its infection of the host insect by disrupting the peritrophic membrane.Journal of virology · 2007Article
- Isolation and characterization of mutants of Pseudomonas maltophila PM-4 altered in chitinolytic activity and antagonistic activity against root rot pathogens of clusterbean (Cyamopsis tetragonoloba).Indian journal of microbiology · 2007Article
- Roles of four chitinases (chia, chib, chic, and chid) in the chitin degradation system of marine bacterium Alteromonas sp. strain O-7.Applied and environmental microbiology · 2005Article
- Incorporation of glucose under anoxic conditions by bacterioplankton from coastal North Sea surface waters.Applied and environmental microbiology · 2005Article
- Detection and characterization of chitinases and other chitin-modifying enzymes.Journal of industrial microbiology & biotechnology · 2003Review
- Genomic analysis and initial characterization of the chitinolytic system of Microbulbifer degradans strain 2-40.Journal of bacteriology · 2003Article
- Molecular analysis of the gene encoding a novel cold-adapted chitinase (ChiB) from a marine bacterium, Alteromonas sp. strain O-7.Journal of bacteriology · 2003Article
- Characterization of chitinase genes from an alkaliphilic actinomycete, Nocardiopsis prasina OPC-131.Applied and environmental microbiology · 2003Article
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Authors and funding
7 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Alteromonas sp. strain O-7 secretes chitinase A (ChiA), chitinase B (ChiB), and chitinase C (ChiC) in the presence of chitin. A gene cluster involved in the chitinolytic system of the strain was cloned and sequenced upstream of and including the chiA gene. The gene cluster consisted of three different open reading frames organized in the order chiD, cbp1, and chiA. The chiD, cbp1, and chiA genes were closely linked and transcribed in the same direction. Sequence analysis indicated that Cbp1 (475 amino acids) was a chitin-binding protein composed of two discrete functional regions. ChiD (1,037 amino acids) showed sequence similarity to bacterial chitinases classified into family 18 of glycosyl hydrolases. The cbp1 and chiD genes were expressed in Escherichia coli, and the recombinant proteins were purified to homogeneity. The highest binding activities of Cbp1 and ChiD were observed when alpha-chitin was used as a substrate. Cbp1 and ChiD possessed a chitin-binding domain (ChtBD) belonging to ChtBD type 3. ChiD rapidly hydrolyzed chitin oligosaccharides in sizes from trimers to hexamers, but not chitin. However, after prolonged incubation with large amounts of ChiD, the enzyme produced a small amount of (GlcNAc)(2) from chitin. The optimum temperature and pH of ChiD were 50 degrees C and 7.0, respectively.
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