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A gene (sleC) encoding a spore-cortex-lytic enzyme from Clostridium perfringens S40 spores; cloning, sequence analysis and molecular characterization

Article Abstract:

The sleC gene encodes a 31 kDa spore-cortex-lytic enzyme from Clostridium perfringens S40. This enzyme prepared as prepro-form, and occurs as an inactive pro-enzyme in the dormant spore which during germination is processed to produce the active enzyme. The amino acid sequence analysis of the 31 kDa enzyme reveals a N-terminal prepro-sequence of 114 amino acid residues, a pro-sequence of 35 amino acid residues and a mature enzyme of 289 amino acid residues. Non-covalent linkage exists between the 36 kDa pro-enzyme and the exterior of the cortex layer.

Author: Miyata, Shigeru, Moriyama, Ryuichi, Miyahara, Nobuko, Makino, Shio
Publisher: Society for General Microbiology
Publication Name: Microbiology
Subject: Biological sciences
ISSN: 1350-0872
Year: 1995
Clostridium

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Primary sequence and enzymic properties of two modular endoglucanases, Cel5A and Cel45A, from the anaerobic fungus Piromyces equi

Article Abstract:

Amino acid sequence of Cel5A and Cel45A endoglucanases resemble family-5 and family-45glycosyl hydrolases respectively. The molecular mass of the endoglucanases are over 194 and 44 kilo daltons and contain four and one catalytic domains respectively. The endoglucanases are part of the high-molecular-mass cellilose-degrading complex of Piromyces equi.

Author: Eberhardt, Ruth Y., Gilbert, Harry J., Hazlewood, Geoffrey P.
Publisher: Society for General Microbiology
Publication Name: Microbiology
Subject: Biological sciences
ISSN: 1350-0872
Year: 2000
Genetic aspects, Fungi, Proteins, Domain structure, Protein conformation

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A novel Cellvibrio mixtus family 10 xylanase that is both intracellular and expressed under non-inducing conditions

Article Abstract:

Results show that xylanase C is localized to the periplasm of the bacterium Cellvibrio mixtus grown on glucose, xylan, and CM-cellulose or Avicel as revealed by antibody probes. Data also indicate that the enzyme exhibits extensive amino acid sequence identity with family 10 xylanases.

Author: Fontes, C.M.G.A., Gilbert, H.J., Hazlewood, G.P., Clarke, J.H., Prates, J.A.M., McKie, V.A., Nagy, T., Fernandes, T.H., Ferreira, L.M.A.
Publisher: Society for General Microbiology
Publication Name: Microbiology
Subject: Biological sciences
ISSN: 1350-0872
Year: 2000
Portugal, Physiological aspects, Plant cell walls, Cell walls, Hydroxylases, Enzyme structure-activity relationships, Saprophytism

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Subjects list: Research, Analysis, Enzymes, Amino acid sequence, Amino acid sequencing, United Kingdom, Statistical Data Included
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