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The Thiamin Pyrophosphate-MotifUsing databases the authors have identified a common thiamin pyrophosphate (TPP)-motif in the family of functionally diverse TPP-dependent enzymes. This common motif consists of multimeric organization of subunits, two catalytic centers, common amino acid sequence, and specific contacts to provide a flip-flop, or alternate site, mechanism of action. Each catalytic center [PP:PYR] is formed at the interface of the PP-domain binding the magnesium ion, pyrophosphate and aminopyrimidine ring of TPP, and the PYR-domain binding the aminopyrimidine ring of that cofactor. A pair of these catalytic centers constitutes the catalytic core [PP:PYR]* within these enzymes. Analysis of the structural elements of this catalytic core reveals novel definition of the common amino acid sequences, which are GX@&(G)@XXGQ, and GDGX25-30 within the PP- domain, and the E&(G)@XXG@ within the PYR-domain, where Q, corresponds to a hydrophobic amino acid. This TPP-motif provides a novel tool for annotation of TPP-dependent enzymes useful in advancing functional proteomics.
Document ID
20040012689
Document Type
Preprint (Draft being sent to journal)
Authors
Dominiak, Paulina M. (NASA Marshall Space Flight Center Huntsville, AL, United States)
Ciszak, Ewa M. (NASA Marshall Space Flight Center Huntsville, AL, United States)
Date Acquired
August 21, 2013
Publication Date
January 1, 2003
Subject Category
Life Sciences (General)
Distribution Limits
Public
Copyright
Work of the US Gov. Public Use Permitted.