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| Content Provider | World Health Organization (WHO)-Global Index Medicus |
|---|---|
| Author | Angelaccio, S. Contestabile, R. Pascarella, S. Di Salvo, M. Bossa, F. Delle Fratte, S. |
| Description | Country affiliation: Italy Author Affiliation: Pascarella S ( Dipartimento di Scienze Biochimiche A. Rossi Fanelli and Centro di Biologia Molecolare del CNR, Università La Sapienza, Roma, Italy.) |
| Abstract | We describe a model for the three-dimensional structure of E. coli serine hydroxymethyltransferase based on its sequence homology with other PLP enzymes of the alpha-family and whose tertiary structures are known. The model suggests that certain amino acid residues at the putative active site of the enzyme can adopt specific roles in the catalytic mechanism. These proposals were supported by analysis of the properties of a number of site-directed mutants. New active site features are also proposed for further experimental testing. |
| ISSN | 09618368 |
| e-ISSN | 1469896X |
| Journal | Protein Science |
| Issue Number | 9 |
| Volume Number | 7 |
| Language | English |
| Publisher | Wiley-Blackwell (on behalf of The Protein Society) |
| Publisher Date | 1998-09-01 |
| Publisher Place | United States |
| Access Restriction | Open |
| Subject Keyword | Escherichia Coli Enzymology Glycine Hydroxymethyltransferase Chemistry Mutagenesis, Site-directed Genetics Amino Acid Sequence Bacterial Proteins Binding Sites Physiology Isoenzymes Models, Molecular Molecular Sequence Data Mutation Protein Structure, Tertiary Pyridoxal Phosphate Sequence Alignment Research Support, Non-u.s. Gov't Discipline Biochemistry |
| Content Type | Text |
| Resource Type | Article |
| Subject | Medicine Molecular Biology Biochemistry |
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