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L-serine production by a methylotroph and its related enzymes.
Appl Microbiol Biotechnol. 1993 Jul; 39(4-5):427-32.AM

Abstract

The production process of L-serine from methanol and glycine has been developed using a methylotroph with the serine pathway. Consecutive reactions of two enzymes, methanol dehydrogenase (MDH) and serine hydroxymethyltransferase (SHMT) are involved in the production. We screened a high producer, Hyphomicrobium methylovorum, which is an obligate methylotroph. With resting cells of the bacterium, 24 mg/ml of L-serine was produced from 100 mg/ml of glycine and 48 mg/ml of methanol in 3 days under optimal conditions. Next, a glycine-resistant mutant GM2 showed improved serine production (32-34 mg/ml). The mutant GM2 was found to have elevated activities of MDH and SHMT. Since there has so far been little report on the systematic characterization of enzymes of the serine pathway in methylotrophs, not only the above two enzymes but also the other three enzymes in H. methylovorum were purified and characterized: MDH, SHMT and hydroxypyruvate reductase (HPR) were crystallized; serine-glyoxylate aminotransferase (SGAT) and glycerate kinase (GK) were purified to homogeneity. As a result, all these enzymes were found to be stable against preservation and to exist abundantly in the bacterium. The gene of SHMT was cloned and its deduced amino acid sequence had homology to those of Escherichia coli (55%) and rabbit liver (44%), whereas the enzyme of the bacterium was immunochemically distinguishable from those of microorganisms other than Hyphomicrobium strains and mammalian livers.

Authors+Show Affiliations

Department of Biotechnology, Tottori University, Japan.No affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info available

Pub Type(s)

Journal Article
Review

Language

eng

PubMed ID

7763921

Citation

Izumi, Y, et al. "L-serine Production By a Methylotroph and Its Related Enzymes." Applied Microbiology and Biotechnology, vol. 39, no. 4-5, 1993, pp. 427-32.
Izumi Y, Yoshida T, Miyazaki SS, et al. L-serine production by a methylotroph and its related enzymes. Appl Microbiol Biotechnol. 1993;39(4-5):427-32.
Izumi, Y., Yoshida, T., Miyazaki, S. S., Mitsunaga, T., Ohshiro, T., Shimao, M., Miyata, A., & Tanabe, T. (1993). L-serine production by a methylotroph and its related enzymes. Applied Microbiology and Biotechnology, 39(4-5), 427-32.
Izumi Y, et al. L-serine Production By a Methylotroph and Its Related Enzymes. Appl Microbiol Biotechnol. 1993;39(4-5):427-32. PubMed PMID: 7763921.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - L-serine production by a methylotroph and its related enzymes. AU - Izumi,Y, AU - Yoshida,T, AU - Miyazaki,S S, AU - Mitsunaga,T, AU - Ohshiro,T, AU - Shimao,M, AU - Miyata,A, AU - Tanabe,T, PY - 1993/7/1/pubmed PY - 1993/7/1/medline PY - 1993/7/1/entrez SP - 427 EP - 32 JF - Applied microbiology and biotechnology JO - Appl. Microbiol. Biotechnol. VL - 39 IS - 4-5 N2 - The production process of L-serine from methanol and glycine has been developed using a methylotroph with the serine pathway. Consecutive reactions of two enzymes, methanol dehydrogenase (MDH) and serine hydroxymethyltransferase (SHMT) are involved in the production. We screened a high producer, Hyphomicrobium methylovorum, which is an obligate methylotroph. With resting cells of the bacterium, 24 mg/ml of L-serine was produced from 100 mg/ml of glycine and 48 mg/ml of methanol in 3 days under optimal conditions. Next, a glycine-resistant mutant GM2 showed improved serine production (32-34 mg/ml). The mutant GM2 was found to have elevated activities of MDH and SHMT. Since there has so far been little report on the systematic characterization of enzymes of the serine pathway in methylotrophs, not only the above two enzymes but also the other three enzymes in H. methylovorum were purified and characterized: MDH, SHMT and hydroxypyruvate reductase (HPR) were crystallized; serine-glyoxylate aminotransferase (SGAT) and glycerate kinase (GK) were purified to homogeneity. As a result, all these enzymes were found to be stable against preservation and to exist abundantly in the bacterium. The gene of SHMT was cloned and its deduced amino acid sequence had homology to those of Escherichia coli (55%) and rabbit liver (44%), whereas the enzyme of the bacterium was immunochemically distinguishable from those of microorganisms other than Hyphomicrobium strains and mammalian livers. SN - 0175-7598 UR - https://www.unboundmedicine.com/medline/citation/7763921/L_serine_production_by_a_methylotroph_and_its_related_enzymes_ L2 - https://www.lens.org/lens/search?q=citation_id:7763921 DB - PRIME DP - Unbound Medicine ER -