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PDBsum entry 1daa
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Transferase (aminotransferase)
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PDB id
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1daa
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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 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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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
perfect match.
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Abstract
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The three-dimensional structure of D-amino acid aminotransferase (D-AAT) in the
pyridoxamine phosphate form has been determined crystallographically. The fold
of this pyridoxal phosphate (PLP)-containing enzyme is completely different from
those of any of the other enzymes that utilize PLP as part of their mechanism
and whose structures are known. However, there are some striking similarities
between the active sites of D-AAT and the corresponding enzyme that
transaminates L-amino acids, L-aspartate aminotransferase. These similarities
represent convergent evolution to a common solution of the problem of enforcing
transamination chemistry on the PLP cofactor. Implications of these similarities
are discussed in terms of their possible roles in the stabilization of
intermediates of a transamination reaction. In addition, sequence similarity
between D-AAT and branched chain L-amino acid aminotransferase suggests that
this latter enzyme will also have a fold similar to that of D-AAT.
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Secondary reference #1
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Title
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Kinetic and stereochemical comparison of wild-Type and active-Site k145q mutant enzyme of bacterial d-Amino acid transaminase.
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Authors
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M.B.Bhatia,
S.Futaki,
H.Ueno,
J.M.Manning,
D.Ringe,
T.Yoshimura,
K.Soda.
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Ref.
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J Biol Chem, 1993,
268,
6932-6938.
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PubMed id
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Secondary reference #2
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Title
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Examination of the function of active site lysine 329 of ribulose-Bisphosphate carboxylase/oxygenase as revealed by the proton exchange reaction.
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Authors
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F.C.Hartman,
E.H.Lee.
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Ref.
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J Biol Chem, 1989,
264,
11784-11789.
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PubMed id
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