[Purification and properties of 3-hexulosephosphate synthase from facultative methylotroph Pseudomonas oleovorans].
Biokhimiia. 1978 May; 43(5):782-8.B

Abstract

3-Hexulosephosphate synthase (HPS), the key enzyme of the hexulosephosphate cycle of formaldehyde fixation, was isolated from facultative methylotroph Pseudomonas oleovorans. Enzyme was purified 100-fold. The purification procedure involved fractionation with ammonium sulfate, gel-filtration on Sephadex G-150 and chromatography on DEAE-Sephadex A-50. The purified enzyme gave single band on analytical polyacrylamide gel electrophoresis. Optimal conditions for activity of HPS are: pH 7,0, temperature 50 degrees C. The molecular weight was calculated to be 45 000 from gel-filtration experiments. HPS is active only in the presence of Mg2+ or Mn2+. Ribulose-5-phosphate is the sole acceptor of formaldehyde. Activity of the enzyme is inhibited by NADH and NADPH.

Authors

Sokolov AP

No affiliation info available

Trotsenko YA

No affiliation info available

MeSH

Aldehyde-LyasesHexosephosphatesKineticsMethaneMolecular WeightPseudomonasRibulosephosphates

Pub Type(s)

Journal Article

Language

rus

PubMed ID

656502

Citation

Sokolov, A P., and Y A. Trotsenko. "[Purification and Properties of 3-hexulosephosphate Synthase From Facultative Methylotroph Pseudomonas Oleovorans]." Biokhimiia (Moscow, Russia), vol. 43, no. 5, 1978, pp. 782-8.

Sokolov AP, Trotsenko YA. [Purification and properties of 3-hexulosephosphate synthase from facultative methylotroph Pseudomonas oleovorans]. Biokhimiia. 1978;43(5):782-8.

Sokolov, A. P., & Trotsenko, Y. A. (1978). [Purification and properties of 3-hexulosephosphate synthase from facultative methylotroph Pseudomonas oleovorans]. Biokhimiia (Moscow, Russia), 43(5), 782-8.

Sokolov AP, Trotsenko YA. [Purification and Properties of 3-hexulosephosphate Synthase From Facultative Methylotroph Pseudomonas Oleovorans]. Biokhimiia. 1978;43(5):782-8. PubMed PMID: 656502.

* Article titles in AMA citation format should be in sentence-case

TY - JOUR T1 - [Purification and properties of 3-hexulosephosphate synthase from facultative methylotroph Pseudomonas oleovorans]. AU - Sokolov,A P, AU - Trotsenko,Y A, PY - 1978/5/1/pubmed PY - 1978/5/1/medline PY - 1978/5/1/entrez SP - 782 EP - 8 JF - Biokhimiia (Moscow, Russia) JO - Biokhimiia VL - 43 IS - 5 N2 - 3-Hexulosephosphate synthase (HPS), the key enzyme of the hexulosephosphate cycle of formaldehyde fixation, was isolated from facultative methylotroph Pseudomonas oleovorans. Enzyme was purified 100-fold. The purification procedure involved fractionation with ammonium sulfate, gel-filtration on Sephadex G-150 and chromatography on DEAE-Sephadex A-50. The purified enzyme gave single band on analytical polyacrylamide gel electrophoresis. Optimal conditions for activity of HPS are: pH 7,0, temperature 50 degrees C. The molecular weight was calculated to be 45 000 from gel-filtration experiments. HPS is active only in the presence of Mg2+ or Mn2+. Ribulose-5-phosphate is the sole acceptor of formaldehyde. Activity of the enzyme is inhibited by NADH and NADPH. SN - 0320-9725 UR - https://www.unboundmedicine.com/medline/citation/656502/[Purification_and_properties_of_3_hexulosephosphate_synthase_from_facultative_methylotroph_Pseudomonas_oleovorans]_ DB - PRIME DP - Unbound Medicine ER -

Tags

[Purification and properties of 3-hexulosephosphate synthase from facultative methylotroph Pseudomonas oleovorans].Biokhimiia. 1978 May; 43(5):782-8.B