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Purification and properties of serine hydroxymethyltransferase from Sulfolobus solfataricus.
J Bacteriol. 1997 Dec; 179(23):7456-61.JB

Abstract

Serine hydroxymethyltransferase (SHMT) catalyzes the reversible cleavage of serine to glycine with the transfer of the one-carbon group to tetrahydrofolate to form 5,10-methylenetetrahydrofolate. No SHMT has been purified from a nonmethanogenic Archaea strain, in part because this group of organisms uses modified folates as the one-carbon acceptor. These modified folates are not readily available for use in assays for SHMT activity. This report describes the purification and characterization of SHMT from the thermophilic organism Sulfolobus solfataricus. The exchange of the alpha-proton of glycine with solvent protons in the absence of the modified folate was used as the activity assay. The purified protein catalyzes the synthesis of serine from glycine and a synthetic derivative of a fragment of the natural modified folate found in S. solfataricus. Replacement of the modified folate with tetrahydrofolate did not support serine synthesis. In addition, this SHMT also catalyzed the cleavage of both allo-threonine and beta-phenylserine in the absence of the modified folate. The cleavage of these two amino acids in the absence of tetrahydrofolate is a property of other characterized SHMTs. The enzyme contains covalently bound pyridoxal phosphate. Sequences of three peptides showed significant similarity with those of peptides of SHMTs from two methanogens.

Authors+Show Affiliations

Department of Biochemistry and Molecular Biophysics, Virginia Commonwealth University, Richmond 23298, USA.No affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info available

Pub Type(s)

Comparative Study
Journal Article
Research Support, Non-U.S. Gov't
Research Support, U.S. Gov't, Non-P.H.S.
Research Support, U.S. Gov't, P.H.S.

Language

eng

PubMed ID

9393711

Citation

Delle Fratte, S, et al. "Purification and Properties of Serine Hydroxymethyltransferase From Sulfolobus Solfataricus." Journal of Bacteriology, vol. 179, no. 23, 1997, pp. 7456-61.
Delle Fratte S, White RH, Maras B, et al. Purification and properties of serine hydroxymethyltransferase from Sulfolobus solfataricus. J Bacteriol. 1997;179(23):7456-61.
Delle Fratte, S., White, R. H., Maras, B., Bossa, F., & Schirch, V. (1997). Purification and properties of serine hydroxymethyltransferase from Sulfolobus solfataricus. Journal of Bacteriology, 179(23), 7456-61.
Delle Fratte S, et al. Purification and Properties of Serine Hydroxymethyltransferase From Sulfolobus Solfataricus. J Bacteriol. 1997;179(23):7456-61. PubMed PMID: 9393711.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Purification and properties of serine hydroxymethyltransferase from Sulfolobus solfataricus. AU - Delle Fratte,S, AU - White,R H, AU - Maras,B, AU - Bossa,F, AU - Schirch,V, PY - 1997/12/11/pubmed PY - 1997/12/11/medline PY - 1997/12/11/entrez SP - 7456 EP - 61 JF - Journal of bacteriology JO - J. Bacteriol. VL - 179 IS - 23 N2 - Serine hydroxymethyltransferase (SHMT) catalyzes the reversible cleavage of serine to glycine with the transfer of the one-carbon group to tetrahydrofolate to form 5,10-methylenetetrahydrofolate. No SHMT has been purified from a nonmethanogenic Archaea strain, in part because this group of organisms uses modified folates as the one-carbon acceptor. These modified folates are not readily available for use in assays for SHMT activity. This report describes the purification and characterization of SHMT from the thermophilic organism Sulfolobus solfataricus. The exchange of the alpha-proton of glycine with solvent protons in the absence of the modified folate was used as the activity assay. The purified protein catalyzes the synthesis of serine from glycine and a synthetic derivative of a fragment of the natural modified folate found in S. solfataricus. Replacement of the modified folate with tetrahydrofolate did not support serine synthesis. In addition, this SHMT also catalyzed the cleavage of both allo-threonine and beta-phenylserine in the absence of the modified folate. The cleavage of these two amino acids in the absence of tetrahydrofolate is a property of other characterized SHMTs. The enzyme contains covalently bound pyridoxal phosphate. Sequences of three peptides showed significant similarity with those of peptides of SHMTs from two methanogens. SN - 0021-9193 UR - https://www.unboundmedicine.com/medline/citation/9393711/Purification_and_properties_of_serine_hydroxymethyltransferase_from_Sulfolobus_solfataricus_ L2 - http://jb.asm.org/cgi/pmidlookup?view=long&pmid=9393711 DB - PRIME DP - Unbound Medicine ER -