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Literature summary extracted from

  • Chen, M.; Cao, J.; Zheng, C.; Liu, Q.
    Directed evolution of an artificial bifunctional enzyme, gamma-glutamyl kinase/gamma-glutamyl phosphate reductase, for improved osmotic tolerance of Escherichia coli transformants (2006), FEMS Microbiol. Lett., 263, 41-47.
    View publication on PubMed

Application

EC Number Application Comment Organism
2.7.2.11 additional information proBA fusion gene and some of the mutated proBA fusion genes can be expressed and functionally complement the proline auxotrophy in Escherichia coli JM83, the fused gamma-glutamyl kinase/gamma-glutamyl phosphate reductase is more active than the separate gamma-glutamyl kinase and gamma-glutamyl phosphate reductase enzymes Bacillus subtilis

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.2.1.41 a fusion of the proA and proB gene of Bacillus subtilis, coding for gamma-glutamyl kinase and gamma-glutamyl phosphate reductase, are cloned for expression of an an artifical bifunctional enzyme in Escherichia coli JM83 Bacillus subtilis
2.7.2.11 proBA fusion gene and mutated proBA fusion gene expressed in Escherichia coli JM83 Bacillus subtilis

Protein Variants

EC Number Protein Variants Comment Organism
2.7.2.11 N177D mutant of the proBA fusion gene, improves the osmotolerance of host cells of Escherichia coli JM83, leads to overproduction of proline by host cells, is about 100fold less sensitive to proline-mediated feedback inhibition than the control Bacillus subtilis

Inhibitors

EC Number Inhibitors Comment Organism Structure
2.7.2.11 L-proline completely inhibits the activity of wild-type gamma-glutamyl kinase/gamma-glutamyl phosphate reductase at concentrations greater than 0.1mM, and inhibits it by 30% at 0.01mM Bacillus subtilis

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.2.1.41 L-glutamate 5-semialdehyde + phosphate + NADP+ Bacillus subtilis
-
L-glutamyl 5-phosphate + NADPH + H+
-
?

Organism

EC Number Organism UniProt Comment Textmining
1.2.1.41 Bacillus subtilis
-
-
-
2.7.2.11 Bacillus subtilis Q6E235
-
-
2.7.2.11 Bacillus subtilis 93151-14 Q6E235
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.7.2.11
-
Bacillus subtilis

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.2.1.41 L-glutamate 5-semialdehyde + phosphate + NADP+
-
Bacillus subtilis L-glutamyl 5-phosphate + NADPH + H+
-
?
2.7.2.11 ATP + L-glutamate
-
Bacillus subtilis ADP + L-glutamate 5-phosphate
-
?
2.7.2.11 ATP + L-glutamate
-
Bacillus subtilis 93151-14 ADP + L-glutamate 5-phosphate
-
?

Synonyms

EC Number Synonyms Comment Organism
1.2.1.41 gamma-glutamyl phosphate reductase
-
Bacillus subtilis
1.2.1.41 gamma-GPR
-
Bacillus subtilis
1.2.1.41 Glutamate-5-semialdehyde dehydrogenase
-
Bacillus subtilis
2.7.2.11 gamma-GK
-
Bacillus subtilis
2.7.2.11 gamma-glutamyl kinase
-
Bacillus subtilis

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
1.2.1.41 25
-
activity assay, room temperature Bacillus subtilis

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.2.1.41 7.2
-
activity assay Bacillus subtilis

Cofactor

EC Number Cofactor Comment Organism Structure
1.2.1.41 NADP+
-
Bacillus subtilis