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Literature summary for 2.4.2.17 extracted from

  • Kulis-Horn, R.K.; Persicke, M.; Kalinowski, J.
    Corynebacterium glutamicum ATP-phosphoribosyl transferases suitable for L-histidine production - Strategies for the elimination of feedback inhibition (2015), J. Biotechnol., 206, 26-37.
    View publication on PubMed
Search for more literature for 2.4.2.17

Cloned(Commentary)

Cloned (Comment) Organism
expressed in Escherichia coli ER2556 cells Corynebacterium glutamicum

Protein Variants

Protein Variants Comment Organism
A249T the mutant is more resistant towards inhibition by L-histidine compared to the wild type enzyme Corynebacterium glutamicum
A270D the mutant with reduced activity is more resistant towards inhibition by L-histidine compared to the wild type enzyme Corynebacterium glutamicum
D213N the mutant is more resistant towards inhibition by L-histidine compared to the wild type enzyme Corynebacterium glutamicum
G230S the mutant is more resistant towards inhibition by L-histidine compared to the wild type enzyme Corynebacterium glutamicum
additional information deletion of the entire C-terminal regulatory domain in combination with the gain of function mutation S143F in the catalytic domain results in an enzyme variant that is still highly active even at L-histidine concentrations close to the solubility limit Corynebacterium glutamicum
S143F the mutant with reduced activity is more resistant towards inhibition by L-histidine compared to the wild type enzyme Corynebacterium glutamicum
S232Y the mutant with increased activity is more resistant towards inhibition by L-histidine compared to the wild type enzyme Corynebacterium glutamicum
S232Y/A270D the mutant with reduced activity is more resistant towards inhibition by L-histidine compared to the wild type enzyme Corynebacterium glutamicum
T228P the mutant is more resistant towards inhibition by L-histidine compared to the wild type enzyme Corynebacterium glutamicum
T235M the mutant is more resistant towards inhibition by L-histidine compared to the wild type enzyme Corynebacterium glutamicum

Inhibitors

Inhibitors Comment Organism Structure
beta-(2-thiazolyl)-DL-alanine
-
 Corynebacterium glutamicum
L-histidine
-
 Corynebacterium glutamicum

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1-(5-phospho-beta-D-ribosyl)-ATP + diphosphate Corynebacterium glutamicum
-
 ATP + 5-phospho-alpha-D-ribose 1-diphosphate
-
 ?
1-(5-phospho-beta-D-ribosyl)-ATP + diphosphate Corynebacterium glutamicum ATCC 13032
-
 ATP + 5-phospho-alpha-D-ribose 1-diphosphate
-
 ?

Organism

Organism UniProt Comment Textmining
Corynebacterium glutamicum Q9Z472
-
-
Corynebacterium glutamicum ATCC 13032 Q9Z472
-
-

Purification (Commentary)

Purification (Comment) Organism
-
 Corynebacterium glutamicum

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1-(5-phospho-beta-D-ribosyl)-ATP + diphosphate
-
 Corynebacterium glutamicum ATP + 5-phospho-alpha-D-ribose 1-diphosphate
-
 ?
1-(5-phospho-beta-D-ribosyl)-ATP + diphosphate
-
 Corynebacterium glutamicum ATCC 13032 ATP + 5-phospho-alpha-D-ribose 1-diphosphate
-
 ?

Synonyms

Synonyms Comment Organism
ATP-phosphoribosyl transferase
-
 Corynebacterium glutamicum
HisG
-
 Corynebacterium glutamicum

Ki Value [mM]

Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
0.0005
-
 L-histidine wild type enzyme, at pH 8.5 and 30°C Corynebacterium glutamicum
0.011
-
 L-histidine mutant enzyme A270D, at pH 8.5 and 30°C Corynebacterium glutamicum
0.022
-
 L-histidine mutant enzyme S232Y, at pH 8.5 and 30°C Corynebacterium glutamicum
0.044
-
 L-histidine mutant enzyme S143F, at pH 8.5 and 30°C Corynebacterium glutamicum
0.178
-
 L-histidine mutant enzyme S232Y/A270D, at pH 8.5 and 30°C Corynebacterium glutamicum