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PMID:20920218

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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

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

Significance

Annotations

Gene product Qualifier GO Term Evidence Code with/from Aspect Extension Notes Status

VIBHA:D9ISE0

enables

GO:0016231: beta-N-acetylglucosaminidase activity

ECO:0000314: direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

VIBHA:D9ISE0

GO:0016231: beta-N-acetylglucosaminidase activity

ECO:0000314:

F

Table 1 shows the kinetic parameters for vhNag2 acting on dfferent GlcNAc substrates.

complete
CACAO 10226

Notes

See also

References

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