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PDBsum entry 2fmj
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References listed in PDB file
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Key reference
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Title
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Conversion of trypsin into a na(+)-Activated enzyme.
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Authors
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M.J.Page,
M.R.Bleackley,
S.Wong,
R.T.Macgillivray,
E.Di cera.
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Ref.
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Biochemistry, 2006,
45,
2987-2993.
[DOI no: ]
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PubMed id
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Abstract
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Serine proteases of the chymotrypsin family show a dichotomous amino acid
distribution for residue 225. Enzymes carrying Tyr at position 225 are activated
by Na(+), whereas those carrying Pro are devoid of Na(+) binding and activation.
Previous studies have demonstrated that the Y225P conversion is sufficient to
abrogate Na(+) activation in several enzymes. However, the reverse substitution
P225Y is necessary but not sufficient to introduce Na(+) binding and activation.
Here we report that Streptomyces griseus trypsin, carrying Pro-225, can be
engineered into a Na(+)-activated enzyme by replacing residues in the 170, 186,
and 220 loops to those of coagulation factor Xa. The findings represent the
first instance of an engineered Na(+)-activated enzyme and a proof of principle
that should enable the design of other proteases with enhanced catalytic
activity and allosteric regulation mediated by monovalent cation binding.
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Secondary reference #1
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Title
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Refined crystal structure of streptomyces griseus trypsin at 1.7 a resolution.
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Authors
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R.J.Read,
M.N.James.
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Ref.
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J Mol Biol, 1988,
200,
523-551.
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PubMed id
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Secondary reference #2
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Title
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Critical evaluation of comparative model building of streptomyces griseus trypsin.
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Authors
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R.J.Read,
G.D.Brayer,
L.Jurásek,
M.N.James.
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Ref.
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Biochemistry, 1984,
23,
6570-6575.
[DOI no: ]
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PubMed id
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Secondary reference #3
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Title
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Engineering the primary substrate specificity of streptomyces griseus trypsin.
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Authors
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M.J.Page,
S.L.Wong,
J.Hewitt,
N.C.Strynadka,
R.T.Macgillivray.
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Ref.
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Biochemistry, 2003,
42,
9060-9066.
[DOI no: ]
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PubMed id
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