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PDBsum entry 1trm
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Hydrolase (serine proteinase)
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PDB id
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1trm
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Contents |
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* Residue conservation analysis
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References listed in PDB file
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Key reference
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Title
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The three-Dimensional structure of asn102 mutant of trypsin: role of asp102 in serine protease catalysis.
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Authors
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S.Sprang,
T.Standing,
R.J.Fletterick,
R.M.Stroud,
J.Finer-Moore,
N.H.Xuong,
R.Hamlin,
W.J.Rutter,
C.S.Craik.
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Ref.
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Science, 1987,
237,
905-909.
[DOI no: ]
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PubMed id
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Abstract
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The structure of the Asn102 mutant of trypsin was determined in order to
distinguish whether the reduced activity of the mutant at neutral pH results
from an altered active site conformation or from an inability to stabilize a
positive charge on the active site histidine. The active site structure of the
Asn102 mutant of trypsin is identical to the native enzyme with respect to the
specificity pocket, the oxyanion hole, and the orientation of the nucleophilic
serine. The observed decrease in rate results from the loss of nucleophilicity
of the active site serine. This decreased nucleophilicity may result from
stabilization of a His57 tautomer that is unable to accept the serine hydroxyl
proton.
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Secondary reference #1
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Title
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The catalytic role of the active site aspartic acid in serine proteases.
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Authors
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C.S.Craik,
S.Roczniak,
C.Largman,
W.J.Rutter.
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Ref.
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Science, 1987,
237,
909-913.
[DOI no: ]
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PubMed id
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