ArticlePloS one2021
The GH19 Engineering Database: Sequence diversity, substrate scope, and evolution in glycoside hydrolase family 19.
Article in PloS one, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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Who cites it
22 citing papers in PubMed.
- Genomic and transcriptomic analysis reveals chitin metabolic pathways in the marine bacterium Microbulbifer harenosus CGMCC 1.13584BMC microbiology · 2026Article
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- Characterization, genomic insights and anti-biofilm potential of phage vB_PaeM_PKMS3, a lytic Pbunavirus capable of infecting clinical Pseudomonas aeruginosa isolates.Antonie van Leeuwenhoek · 2026Article
- Characterization of an Atypical GH19 Family Chitinase fromMicroorganisms · 2026Article
- Green bioconversion of insoluble chitin: chitinase development pathways via multi-strategy synergy.Bioresources and bioprocessing · 2026Review
- Genomic landscape of biosynthetic gene clusters in Iranian extremophiles reveals prolific metabolite potential, prophage associations, and integrated defensive-metabolic islands.BMC microbiology · 2026Article
- Unveiling the antibacterial effects of endolysin POE and holin Hol8 from Pseudomonas otitidis phage vB_PotS-PotUPM1.World journal of microbiology & biotechnology · 2026Article
- Isolation and Characterization of A Novel Pbunavirus with Promising Antibiofilm Activity Against Pseudomonas Aeruginosa.Current microbiology · 2025Article
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- Expression of endochitinase and exochitinase in lettuce chloroplasts increases plant biomass and kills fungal pathogen Candida albicans.Plant biotechnology journal · 2025Article
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- Two novel phages infectingFrontiers in microbiology · 2025Article
- A crucial active site network of titratable residues guides catalysis and NADProtein science : a publication of the Protein Society · 2025Article
- Transcriptomic insights into arabinogalactan protein mechanism of action in galactosyltransferase octuple mutants.Frontiers in plant science · 2025Article
- Characterization of the chitinase gene family in Saccharum reveals the disease resistance mechanism of ScChiVII1.Plant cell reports · 2024Article
- Genome-Wide Identification of a Maize Chitinase Gene Family and the Induction of Its Expression byGenes · 2024Article
- Gene functions of theMicrobial genomics · 2024Article
- Chitinolytic and Fungicidal Potential of the Marine Bacterial Strains Habituating Pacific Ocean Regions.Microorganisms · 2023Article
- An objective criterion to evaluate sequence-similarity networks helps in dividing the protein family sequence space.PLoS computational biology · 2023Article
- Recombinant Thaumatin-Like Protein (rTLP) and Chitinase (rCHI) fromMolecules (Basel, Switzerland) · 2022Article
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4 authors.
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Abstract
The glycoside hydrolase 19 (GH19) is a bifunctional family of chitinases and endolysins, which have been studied for the control of plant fungal pests, the recycle of chitin biomass, and the treatment of multi-drug resistant bacteria. The GH19 domain-containing sequences (22,461) were divided into a chitinase and an endolysin subfamily by analyzing sequence networks, guided by taxonomy and the substrate specificity of characterized enzymes. The chitinase subfamily was split into seventeen groups, thus extending the previous classification. The endolysin subfamily is more diverse and consists of thirty-four groups. Despite their sequence diversity, twenty-six residues are conserved in chitinases and endolysins, which can be distinguished by two specific sequence patterns at six and four positions, respectively. Their location outside the catalytic cleft suggests a possible mechanism for substrate specificity that goes beyond the direct interaction with the substrate. The evolution of the GH19 catalytic domain was investigated by large-scale phylogeny. The inferred evolutionary history and putative horizontal gene transfer events differ from previous works. While no clear patterns were detected in endolysins, chitinases varied in sequence length by up to four loop insertions, causing at least eight distinct presence/absence loop combinations. The annotated GH19 sequences and structures are accessible via the GH19 Engineering Database (GH19ED, https://gh19ed.biocatnet.de). The GH19ED has been developed to support the prediction of substrate specificity and the search for novel GH19 enzymes from neglected taxonomic groups or in regions of the sequence space where few sequences have been described yet.
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