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Literature summary for 6.3.1.2 extracted from

  • Dabrowski, M.J.; Dietze, E.C.; Atkins, W.M.
    Engineering the aggregation properties of dodecameric glutamine synthetase: a single amino acid substitution controls salting out (1996), Protein Eng., 9, 291-298.
    View publication on PubMed
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Protein Variants

Protein Variants Comment Organism
H12D each of the mutant proteins H4A, H4C, M8L, H12L, H12D retains an intact dodecameric ring structure and no significant changes in catalytic and regulatory behavior are caused by the amino acid substitutions on the dodecamer surface. The substitution Ala4His completely abolishes the (NH4)2SO4-induced aggregation. However the H4C mutant protein precipitates nearly completely under the same salting out conditions Escherichia coli
H12L each of the mutant proteins H4A, H4C, M8L, H12L, H12D retains an intact dodecameric ring structure and no significant changes in catalytic and regulatory behavior are caused by the amino acid substitutions on the dodecamer surface. The substitution Ala4His completely abolishes the (NH4)2SO4-induced aggregation. However the H4C mutant protein precipitates nearly completely under the same salting out conditions Escherichia coli
H4A each of the mutant proteins H4A, H4C, M8L, H12L, H12D retains an intact dodecameric ring structure and no significant changes in catalytic and regulatory behavior are caused by the amino acid substitutions on the dodecamer surface. The substitution Ala4His completely abolishes the (NH4)2SO4-induced aggregation. However the H4C mutant protein precipitates nearly completely under the same salting out conditions Escherichia coli
H4C each of the mutant proteins H4A, H4C, M8L, H12L, H12D retains an intact dodecameric ring structure and no significant changes in catalytic and regulatory behavior are caused by the amino acid substitutions on the dodecamer surface. The substitution Ala4His completely abolishes the (NH4)2SO4-induced aggregation. However the H4C mutant protein precipitates nearly completely under the same salting out conditions Escherichia coli
M8L each of the mutant proteins H4A, H4C, M8L, H12L, H12D retains an intact dodecameric ring structure and no significant changes in catalytic and regulatory behavior are caused by the amino acid substitutions on the dodecamer surface. The substitution Ala4His completely abolishes the (NH4)2SO4-induced aggregation. However the H4C mutant protein precipitates nearly completely under the same salting out conditions Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
 wild-type and site-directed mutants H4A, H4C, M8L, H12L, H12D
-

Purification (Commentary)

Purification (Comment) Organism
-
 Escherichia coli

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + L-Glu + NH4+
-
 Escherichia coli ADP + phosphate + L-Gln
-
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