Similarity between serine hydroxymethyltransferase and other pyridoxal phosphate‐dependent enzymes

FEBS Letters

Bossa, Francesco²  Schirch, Verne¹  Pascarella, Stefano² 

[1] Department of Biochemistry and Molecular Biophysics, Virginia Commonwealth University, Richmond, VA 23298, USA;Dipartimento di Scienze Biochimiche A Rossi Fanelli, Centro di Biologia, Molecolare del Consiglio Nazionale delie Ricerche, Università La Sapienza, 00185 Roma, Italy

关键词: Profile analysis;    Site-directed mutagenesis;    Pyridoxal-phosphate;    Aminotransferase;    Serine hydroxymethyltransferase;    Dialkylglycine decarboxylase;    Structure superposition;    PLP;    pyridoxal-5'-phosphate;    AAT;    aspartate aminotransferases;    mCAAT;    mitochondrial chicken AAT;    DGD;    dialkylglycine decarboxylase;    SHMT;    serine hydroxymethyltransferase;    PDB;    Protein Data Bank;   

DOI  :  10.1016/0014-5793(93)80314-K

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

A structural homology of the pyridoxal-5'-phosphate (PLP)-dependent enzyme serine hydroxymethyltransferase (SHMT) with aspartate aminotransferase (AAT) is proposed. Although the two sequences are very dissimilar, a reasonable alignment was obtained using the profile analysis method. Sequences of AAT and dialkylglycine decarboxylase (DGD), for which crystal structure data are available, have been aligned on the basis of their structure superposition. A profile was then calculated and SHMT sequence aligned to it. Three of the four residues conserved in all aminotransferases (including the PLP-binding lysine) are matched. A profile search with DGD-AAT-SHMT profile is more selective and sensitive than individual sequence profiles for PLP-dependent enzyme detection. Potential homologies with the eryCl gene product involved in erythromycin biosynthesis and with amino acid decarboxylases were observed. Homology with AAT will be used as a guideline for planning site-directed mutagenesis experiments on SHMT.

【 授权许可】

Unknown