Abstract
Chaetomium globosum endo-1,4-beta-xylanase (XylCg) is distinguished from other xylanases by its high turnover rate (1,860 s(-1)), the highest ever reported for fungal xylanases. One conserved amino acid, W48, in the substrate binding pocket of wild-type XylCg was identified as an important residue affecting XylCg's catalytic efficiency.
Original language | English |
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Journal | Applied and Environmental Microbiology |
Volume | 78 |
Issue number | 24 |
Pages (from-to) | 8817-8821 |
ISSN | 0099-2240 |
DOIs | |
Publication status | Published - 2012 |
Externally published | Yes |
Keywords
- catalytic efficiency
- energetics
- enzyme activity
- sigma pi interaction
- turnover rate
- Algae Plantae (Algae, Microorganisms, Nonvascular Plants, Plants) - Chlorophyta [13300] Chaetosphaeridium globosum species
- Fungi Plantae (Fungi, Microorganisms, Nonvascular Plants, Plants) - Ascomycetes [15100] Chaetomium globosum species
- Fungi Plantae (Fungi, Microorganisms, Nonvascular Plants, Plants) - Fungi Imperfecti or Deuteromycetes [15500] Aspergillus niger species Trichoderma reesei species Aspergillus versicolor species Trichoderma genus strain-SY
- endo-1,4-beta-xylanase XylCg EC 3.2.1.8
- 03504, Genetics - Plant
- 10062, Biochemistry studies - Nucleic acids, purines and pyrimidines
- 10802, Enzymes - General and comparative studies: coenzymes
- 51518, Plant physiology - Enzymes
- Biochemistry and Molecular Biophysics
- 4386742 GenBank, EMBL, DDJB nucleotide sequence
- Enzymology
- Amino Acid Sequence
- Amino Acid Substitution
- Amino Acids
- Catalytic Domain
- Chaetomium
- Endo-1,4-beta Xylanases
- Kinetics
- Models, Molecular
- Molecular Sequence Data
- EC 3.2.1.8 Endo-1,4-beta Xylanases
- Biotechnology
- Microbiology
- Amino acids
- amino acid
- endo 1,4 beta xylanase
- catalyst
- chemical binding
- fungus
- substrate
- amino acid sequence
- amino acid substitution
- article
- chemical structure
- enzyme active site
- enzymology
- genetics
- kinetics
- metabolism
- molecular genetics
- Chaetomium globosum
- Catalytic efficiencies
- Substrate binding
- Turnover rate
- Wild types
- Xylanases
- BIOTECHNOLOGY
- MICROBIOLOGY
- TRICHODERMA-REESEI
- SUBSTRATE-BINDING
- XYLANASE
- SITE
- FAMILY-11
- SUBSITES
- CHAETOMIUM globosum
- Environmental Microbiology