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PMID:20920218
Citation |
Suginta, W, Chuenark, D, Mizuhara, M and Fukamizo, T (2010) Novel β-N-acetylglucosaminidases from Vibrio harveyi 650: cloning, expression, enzymatic properties, and subsite identification. BMC Biochem. 11:40 |
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Abstract |
Since chitin is a highly abundant natural biopolymer, many attempts have been made to convert this insoluble polysaccharide into commercially valuable products using chitinases and β-N-acetylglucosaminidases (GlcNAcases). We have previously reported the structure and function of chitinase A from Vibrio harveyi 650. This study t reports the identification of two GlcNAcases from the same organism and their detailed functional characterization. |
Links |
PubMed PMC2955587 Online version:10.1186/1471-2091-11-40 |
Keywords |
Acetylglucosaminidase/chemistry; Acetylglucosaminidase/genetics; Acetylglucosaminidase/metabolism; Amino Acid Sequence; Biocatalysis; Chitin/metabolism; Cloning, Molecular; Hydrolysis; Kinetics; Molecular Sequence Data; Recombinant Proteins/chemistry; Recombinant Proteins/genetics; Recombinant Proteins/metabolism; Sequence Alignment; Substrate Specificity; Vibrio/enzymology |
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Significance
Annotations
Gene product | Qualifier | GO Term | Evidence Code | with/from | Aspect | Extension | Notes | Status |
---|---|---|---|---|---|---|---|---|
enables |
GO:0016231: beta-N-acetylglucosaminidase activity |
ECO:0000314: direct assay evidence used in manual assertion |
F |
Seeded From UniProt |
complete | |||
GO:0016231: beta-N-acetylglucosaminidase activity |
ECO:0000314: |
F |
Table 1 shows the kinetic parameters for vhNag2 acting on dfferent GlcNAc substrates. |
complete | ||||
Notes
See also
References
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