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Molecular organization of the alkali-insoluble fraction of Aspergillus fumigatus cell wall.
- T. Fontaine, C. Simenel, +6 authors J. P. Latgé
- Biology, Medicine
- The Journal of biological chemistry
- 8 September 2000
Physical and biological properties of the fungal cell wall are determined by the composition and arrangement of the structural polysaccharides. Cell wall polymers of fungi are classically divided… Expand
High resolution structural analyses of mutant chitinase A complexes with substrates provide new insight into the mechanism of catalysis.
- Y. Papanikolau, G. Prag, G. Tavlas, C. Vorgias, A. Oppenheim, K. Petratos
- Chemistry, Medicine
- 31 August 2001
Chitinase A (ChiA) from the bacterium Serratia marcescens is a hydrolytic enzyme, which cleaves beta-1,4-glycosidic bonds of the natural biopolymer chitin to generate di-N-acetyl-chitobiose. The… Expand
Crystal structure of a bacterial chitinase at 2.3 A resolution.
BACKGROUND Chitinases cleave the beta-1-4-glycosidic bond between the N-acetyl-D-glucosamine units of which chitin is comprised. Chitinases are present in plants, bacteria and fungi, but whereas… Expand
Evolutionary divergence and conservation of trypsin.
The trypsin sequences currently available in the data banks have been collected and aligned using first the amino acid sequence homology and, subsequently, the superposed crystal structures of… Expand
Molecular analysis of the gene encoding a new chitinase from the marine psychrophilic bacterium Moritella marina and biochemical characterization of the recombinant enzyme
The marine psychrophilic bacterium Moritella marina, isolated from a sample raised from a depth of 1,200 m in the northern Pacific Ocean, secretes several chitinases in response to chitin induction.… Expand
Characterization of a cell-wall acid phosphatase (PhoAp) in Aspergillus fumigatus.
In the filamentous fungus Aspergillus fumigatus, the vast majority of the cell-wall-associated proteins are secreted proteins that are in transit in the cell wall. These proteins can be solubilized… Expand
Molecular cloning, structural analysis, and expression in Escherichia coli of a chitinase gene from Enterobacter agglomerans.
- L. Chernin, L. De La Fuente, +4 authors I. Chet
- Biology, Medicine
- Applied and environmental microbiology
- 1 March 1997
The gene chiA, which codes for endochitinase, was cloned from a soilborne Enterobacter agglomerans. Its complete sequence was determined, and the deduced amino acid sequence of the enzyme designated… Expand
N-Acetylglucosaminidase (chitobiase) from Serratia marcescens: gene sequence, and protein production and purification in Escherichia coli.
The chitobiase (Chb) encoding gene (chb) from Serratia marcescens (Sm) has been cloned, sequenced and expressed in Escherichia coli (Ec). Sequencing has revealed an open reading frame encodinga… Expand
Purification and characterization of a new hyperthermostable, allosamidin-insensitive and denaturation-resistant chitinase from the hyperthermophilic archaeon Thermococcus chitonophagus
Abstract. A new chitinase (1,4-β-D-N-acetyl-glucosaminidase, EC 126.96.36.199) was detected and purified to homogeneity in its native form from the chitinolytic enzyme system of the extremely thermophilic… Expand
Cloning and primary structure of the chiA gene from Aeromonas caviae.
The chiA gene from Aeromonas caviae encodes an extracellular chitinase, 865 amino acids long, that shows a high degree of similarity to chitinase A of Serratia marcescens. Expression in Escherichia… Expand