Conserved sequence pattern in a wide variety of phosphoesterases
Open Access
- 1 February 1994
- journal article
- for the-record
- Published by Wiley in Protein Science
- Vol. 3 (2), 356-358
- https://doi.org/10.1002/pro.5560030218
Abstract
A unique sequence pattern, designated the GD/GNH signature, was shown to be conserved in a wide variety of phosphoesterases. The enzymes containing this signature cleave phosphoester bonds in such different substrates as (1) phosphoserine and phosphothreonine in polypeptides; (2) bis(5′‐nucleosidyl)‐tetraphosphates; (3) nucleoside 5′ phosphates; (4) 2′,3′‐cyclic nucleotide phosphates; (5) polynucleotides; (6) 2′‐5′ phospho‐diesters in RNA (intron) lariats; (7) sphingomyelin; and (7) various phosphomonoesters. Two conserved acidic amino acid residues and a conserved histidine residue may be directly involved in phosphoester bond cleavage.Keywords
This publication has 19 references indexed in Scilit:
- The PROSITE dictionary of sites and patterns in proteins, its current statusNucleic Acids Research, 1993
- Bacterial and bacteriophage protein phosphatasesMolecular Microbiology, 1993
- Location of theBacillus subtilis sbcDgene downstream of addAB, the analogues ofE.coli recBCNucleic Acids Research, 1993
- Isolation and characterization of the gene encoding yeast debranching enzymeCell, 1991
- A workbench for multiple alignment construction and analysisProteins-Structure Function and Bioinformatics, 1991
- Basic local alignment search toolJournal of Molecular Biology, 1990
- Design and characterization of Escherichia coli mutants devoid of Ap4N-hydrolase activityJournal of Molecular Biology, 1990
- Evolution of a bifunctional enzyme: 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase.Proceedings of the National Academy of Sciences, 1989
- Two early genes of bacteriophage T5 encode proteins containing an NTP-binding sequence motif and probably involved in DNA replication, recombination and repairFEBS Letters, 1989
- THE STRUCTURE AND REGULATION OF PROTEIN PHOSPHATASESAnnual Review of Biochemistry, 1989