Summary
3-Hexulose phosphate synthase was purified in 94% yield from Methylomonas M15. The enzyme did not form a Schiff-base intermediate with d-ribulose 5-phosphate that could be reduced by NaBH4. However, the enzyme required Mg2+ or Mn2+ ions for activity and was inactivated in the presence of EDTA. The latter is a property of class II aldolases. The enzyme accepted a wide range of other aldehydes in addition to its natural substrate formaldehyde, while d-ribulose 5-phosphate could not be replaced. This makes it an attractive tool for the synthesis of higher sugar phosphates.
This is a preview of subscription content, log in via an institution to check access.
Similar content being viewed by others
References
Bednarski MD, Simon ES, Bischofsberger N, Fessner W-D, Kim M-J, Lees W, Saito T, Waldman H, Whitesides GM (1989) Rabbit muscle aldolase as a catalyst in organic synthesis. J Am Chem Soc 111:627–635
Bradford MM (1976) A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem 72:248–254
Commission of the European Community (1982) Amtsblatt der Europäischen Gemeinschaften NP. L 185/18 185/22 vom 30. 6. 82
Ferenci T, Strøm T, Quayle JR (1974) Purification and properties of 3-hexulose phosphate synthase and phospho-3-hexuloisomerase from Methylococcus capsulatus. Biochem J 144:477–486
Hanes CS, Isherwood FA (1949) Separation of the phosphoric esters on the filter paper chromatogram. Nature 164:1102–1107
Horecker BL, Tsolas O, Lai CY (1972) Aldolases. In: Boyer PD (ed) The enzymes, vol. 7, 3rd edn. Academic press, New York, pp 213–258
Kato N, Ohashi H, Tani Y, Ogata K (1978) 3-Hexulose-phosphate synthase from Methylomonas aminofaciens 77a. Biochim Biophys Acta 523:236–244
Kato N, Miyamoto N, Shimao M, Sakazawa C (1988) 3-Hexulose-phosphate synthase from a new facultative methylotroph Mycobacterium gastri MB19. Agric Biol Chem 52:2659–2661
Kemp MB (1972) The hexose phosphate synthetase of Methylococcus capsulatus. Biochem J 127:64–65
Laemmli UK (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227:680–685
Large PJ, Bamforth CH (1988) Methylotrophy and biotechnology. Longman Scientific and Technical, Burnt Mill, Harlow, UK
Nash T (1953) The colorimetric estimation of formaldehyde by means of the Hantzsch-reaction. Biochem J 55:416–421
Quayle JR (1972) The metabolism of one-carbon compounds by microorganisms. Adv Microb Physiol 7:119–203
Rutter WJ (1964) Evolution of aldolase. Fed Proc 23:1248–1257
Sahm H, Wagner F (1975) Isolation and characterization of an obligate methanol-utilizing bacterium Metylomonas M15. Eur J Appl Microbiol 2:147–158
Sahm H, Schütte H, Kula M-R (1976) Purification and properties of 3-hexulosephosphate synthase from Methylomonas M15. Eur J Biochem 66:591–596
Ziegler T, Straub A, Effenberger F (1988) Enzym-katalysierte Synthese von 1-Desoxymannojirimycin, 1-Desoxynojirimycin und 1,4-Didesoxy-1,4-imino-d-arabinitol. Angew Chem 100:737–738
Author information
Authors and Affiliations
Additional information
Offprint requests to: M.-R. Kula
Rights and permissions
About this article
Cite this article
Beisswenger, R., Kula, MR. Catalytic properties and substrate specificity of 3-hexulose phosphate synthase fromMethylomonas M15. Appl Microbiol Biotechnol 34, 604–607 (1991). https://doi.org/10.1007/BF00167907
Received:
Accepted:
Issue Date:
DOI: https://doi.org/10.1007/BF00167907