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Characterization of a serine hydroxymethyltransferase for L-serine enzymatic production from Pseudomonas plecoglossicida.
World J Microbiol Biotechnol. 2013 Nov; 29(11):2067-76.WJ

Abstract

Pseudomonas plecoglossicida, a bacterium strain that exhibits high Serine hydroxymethyltransferase (SHMT) activity, was isolated from the seawater. A full-length glyA encoding SHMT was obtained by a modified thermal asymmetric interlaced-PCR (TRIL-PCR), which consisted of 1,254 bp, encoded a 417 amino acid polypeptide, and shared the highest identity (75 %) with a glyA gene from Acinetobacter radioresistens CMC-1. Recombinant glyA gene was expressed in Escherichia coli BL21 (DE3) and purified by electrophoretic homogeneity. The enzyme showed the optimal activity at pH 8.0 and 40 °C, and remained stable in high alkali conditions. Using SHMT to produce L-serine by catalyzing the reaction of glycine and tetrahydrofolate is one of the most promising routes to synthesize L-serine, achieving 33.4 mM L-serine at the 12th h of the enzymatic reaction with the substrates of glycine (133 mM) and formaldehyde (13.3 mM). The properties make the SHMT a candidate for further enzymatic studies and industrial applications.

Authors+Show Affiliations

State Key Laboratory of Agricultural Microbiology, College of Life Science and Technology, Huazhong Agricultural University, Wuhan, 430070, People's Republic of China.No affiliation info availableNo affiliation info availableNo affiliation info available

Pub Type(s)

Journal Article
Research Support, Non-U.S. Gov't

Language

eng

PubMed ID

23913024

Citation

Jiang, Wei, et al. "Characterization of a Serine Hydroxymethyltransferase for L-serine Enzymatic Production From Pseudomonas Plecoglossicida." World Journal of Microbiology & Biotechnology, vol. 29, no. 11, 2013, pp. 2067-76.
Jiang W, Xia B, Huang J, et al. Characterization of a serine hydroxymethyltransferase for L-serine enzymatic production from Pseudomonas plecoglossicida. World J Microbiol Biotechnol. 2013;29(11):2067-76.
Jiang, W., Xia, B., Huang, J., & Liu, Z. (2013). Characterization of a serine hydroxymethyltransferase for L-serine enzymatic production from Pseudomonas plecoglossicida. World Journal of Microbiology & Biotechnology, 29(11), 2067-76. https://doi.org/10.1007/s11274-013-1370-9
Jiang W, et al. Characterization of a Serine Hydroxymethyltransferase for L-serine Enzymatic Production From Pseudomonas Plecoglossicida. World J Microbiol Biotechnol. 2013;29(11):2067-76. PubMed PMID: 23913024.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Characterization of a serine hydroxymethyltransferase for L-serine enzymatic production from Pseudomonas plecoglossicida. AU - Jiang,Wei, AU - Xia,Bingzhao, AU - Huang,Junjie, AU - Liu,Ziduo, Y1 - 2013/08/03/ PY - 2013/02/26/received PY - 2013/05/03/accepted PY - 2013/8/6/entrez PY - 2013/8/6/pubmed PY - 2014/5/3/medline SP - 2067 EP - 76 JF - World journal of microbiology & biotechnology JO - World J. Microbiol. Biotechnol. VL - 29 IS - 11 N2 - Pseudomonas plecoglossicida, a bacterium strain that exhibits high Serine hydroxymethyltransferase (SHMT) activity, was isolated from the seawater. A full-length glyA encoding SHMT was obtained by a modified thermal asymmetric interlaced-PCR (TRIL-PCR), which consisted of 1,254 bp, encoded a 417 amino acid polypeptide, and shared the highest identity (75 %) with a glyA gene from Acinetobacter radioresistens CMC-1. Recombinant glyA gene was expressed in Escherichia coli BL21 (DE3) and purified by electrophoretic homogeneity. The enzyme showed the optimal activity at pH 8.0 and 40 °C, and remained stable in high alkali conditions. Using SHMT to produce L-serine by catalyzing the reaction of glycine and tetrahydrofolate is one of the most promising routes to synthesize L-serine, achieving 33.4 mM L-serine at the 12th h of the enzymatic reaction with the substrates of glycine (133 mM) and formaldehyde (13.3 mM). The properties make the SHMT a candidate for further enzymatic studies and industrial applications. SN - 1573-0972 UR - https://www.unboundmedicine.com/medline/citation/23913024/Characterization_of_a_serine_hydroxymethyltransferase_for_L_serine_enzymatic_production_from_Pseudomonas_plecoglossicida_ L2 - https://dx.doi.org/10.1007/s11274-013-1370-9 DB - PRIME DP - Unbound Medicine ER -