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Structural studies of a Phe256Trp mutant of human salivary α-amylase: Implications for the role of a conserved water molecule in enzyme activity
Narayanan Ramasubbu
, Krishnan Sundar
, Chandran Ragunath
, Mohamed M. Rafi
School of Dental Medicine, Oral Biology
Rutgers, The State University
Research output
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Contribution to journal
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Article
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peer-review
17
Scopus citations
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Dive into the research topics of 'Structural studies of a Phe256Trp mutant of human salivary α-amylase: Implications for the role of a conserved water molecule in enzyme activity'. Together they form a unique fingerprint.
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Keyphrases
Enzyme Activity
100%
Amylase
100%
Salivary alpha-amylase
100%
Conserved Water Molecules
100%
Water Molecule
66%
Starch
66%
Complex Structure
33%
X-ray Structure
33%
Specific Activity
33%
4-fold
33%
Amino
33%
Kinetic Analysis
33%
Catalytic Residues
33%
Kcat
33%
Hydrolysis Mechanism
33%
Hydroxyethyl
33%
Amylase Activity
33%
Water Chain
33%
Positional Change
33%
1,3-Propanediol
33%
Biochemistry, Genetics and Molecular Biology
Enzyme Activity
100%
Koji
100%
Starch
28%
X Ray
14%
Enzymatic Hydrolysis
14%
Kinetics
14%
Turnover Number
14%