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PDBsum entry 2dab
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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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Crystal structures of l201a mutant of d-Amino acid aminotransferase at 2.0 a resolution: implication of the structural role of leu201 in transamination.
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Authors
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S.Sugio,
A.Kashima,
K.Kishimoto,
D.Peisach,
G.A.Petsko,
D.Ringe,
T.Yoshimura,
N.Esaki.
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Ref.
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Protein Eng, 1998,
11,
613-619.
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PubMed id
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Note In the PDB file this reference is
annotated as "TO BE PUBLISHED".
The citation details given above were identified by an automated
search of PubMed on title and author
names, giving a
percentage match of
94%.
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Abstract
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The leucine-to-alanine mutation at residue 201 of D-amino acid aminotransferase
provides a unique enzyme which gradually loses its activity while catalyzing the
normal transamination; the co-enzyme form is converted from pyridoxal
5'-phosphate to pyridoxamine 5'-phosphate upon the inactivation [Kishimoto,K.,
Yoshimura,T., Esaki,N., Sugio,S., Manning,J.M. and Soda,K. (1995) J. Biochem.,
117, 691-696]. Crystal structures of both co-enzyme forms of the mutant enzyme
have been determined at 2.0 A resolution: they are virtually identical, and are
quite similar to that of the wild-type enzyme. Significant differences in both
forms of the mutant are localized only on the bound co-enzyme, the side chains
of Lys145 and Tyr31, and a water molecule sitting on the putative substrate
binding site. Detailed comparisons of the structures of the mutant, together
with that of the pyridoxamine-5'-phosphate form of the wild-type enzyme, imply
that Leu201 would play a crucial role in the transamination reaction by keeping
the pyridoxyl ring in the proper location without disturbing its oscillating
motion, although the residue seems to not be especially important for the
structural integrity of the enzyme.
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Secondary reference #1
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Title
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Role of leucine 201 of thermostable d-Amino acid aminotransferase from a thermophile, Bacillus sp. Ym-1.
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Authors
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K.Kishimoto,
T.Yoshimura,
N.Esaki,
S.Sugio,
J.M.Manning,
K.Soda.
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Ref.
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J Biochem (tokyo), 1995,
117,
691-696.
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PubMed id
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Secondary reference #2
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Title
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Crystal structure of a d-Amino acid aminotransferase: how the protein controls stereoselectivity.
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Authors
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S.Sugio,
G.A.Petsko,
J.M.Manning,
K.Soda,
D.Ringe.
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Ref.
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Biochemistry, 1995,
34,
9661-9669.
[DOI no: ]
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PubMed id
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