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Literature summary for 2.1.2.1 extracted from

  • Zhao, G.H.; Li, H.; Liu, W.; Zhang, W.G.; Zhang, F.; Liu, Q.; Jiao, Q.C.
    Preparation of optically active beta-hydroxy-alpha-amino acid by immobilized Escherichia coli cells with serine hydroxymethyl transferase activity (2011), Amino Acids, 40, 215-220.
    View publication on PubMed
Search for more literature for 2.1.2.1

Application

Application Comment Organism
synthesis improved method for preparation of optically pure beta-hydroxy-alpha-amino acids, catalyzed by serine hydroxymethyl transferase with threonine aldolase activity. Usage of substrates beta-phenylserine, beta-(nitrophenyl) serine and beta-(methylsulfonylphenyl) serine with immobilized recombinant enzyme for SHMT activity, optimal at pH 7.5 and 45°C. The immobilized cells are continuously used 10 times, yielding an average conversion rate of 60.4% Escherichia coli

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli strain BL21 (DE3) Escherichia coli

Protein Variants

Protein Variants Comment Organism
additional information immobilization of cells using 3% alginate (w/v), 5 g cells (wet), and 2% (w/v) CaCl2 solution Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-
Escherichia coli K-12 MG1655
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information SHMT activity with beta-phenylserine as substrate is about 1.48fold and 1.25fold higher than that with beta-(methylsulfonylphenyl) serine and beta-(nitrophenyl) serine as substrate, respectively. Besides SHMT activity, the enzyme also shows L-allo-threonine aldolase activity, EC 4.1.2.48 Escherichia coli ?
-
 ?
additional information SHMT activity with beta-phenylserine as substrate is about 1.48fold and 1.25fold higher than that with beta-(methylsulfonylphenyl) serine and beta-(nitrophenyl) serine as substrate, respectively. Besides SHMT activity, the enzyme also shows L-allo-threonine aldolase activity, EC 4.1.2.48 Escherichia coli K-12 MG1655 ?
-
 ?

Synonyms

Synonyms Comment Organism
serine hydroxymethyl transferase
-
 Escherichia coli
SHMT
-
 Escherichia coli

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
45
-
-
 Escherichia coli

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.5
-
-
 Escherichia coli

pH Range

pH Minimum pH Maximum Comment Organism
4 10 activity range Escherichia coli

Cofactor

Cofactor Comment Organism Structure
pyridoxal 5'-phosphate dependent on Escherichia coli