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Similarity between serine hydroxymethyltransferase and other pyridoxal phosphate‐dependent enzymes
Author(s) -
Pascarella Stefano,
Schirch Verne,
Bossa Francesco
Publication year - 1993
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(93)80314-k
Subject(s) - serine hydroxymethyltransferase , biochemistry , enzyme , serine , pyridoxal phosphate , biology , homology (biology) , amino acid , lysine decarboxylase , cofactor , putrescine , cadaverine
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.