Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 6.3.4.13 extracted from

  • Wang, W.; Kappock, T.J.; Stubbe, J.; Ealick, S.E.
    X-ray crystal structure of glycinamide ribonucleotide synthetase from Escherichia coli (1998), Biochemistry, 37, 15647-15662.
    View publication on PubMed
Search for more literature for 6.3.4.13

Cloned(Commentary)

Cloned (Comment) Organism
expressed as the selenomethionine incorporated protein Escherichia coli

Crystallization (Commentary)

Crystallization (Comment) Organism
selenomethionine incorporated enzyme, hanging drop vapor diffusion method Escherichia coli

Protein Variants

Protein Variants Comment Organism
P294L loss of function Escherichia coli

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
48240
-
 calculated from amino acid sequence Escherichia coli
49000
-
 gel filtration Escherichia coli

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Escherichia coli second step in de novo purine biosynthesis pathway ?
-
 ?

Organism

Organism UniProt Comment Textmining
Escherichia coli P15640
-
-

Purification (Commentary)

Purification (Comment) Organism
-
 Escherichia coli

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
2.3
-
 selenomethionine-substituted enzyme Escherichia coli
19
-
 methionine-substituted enzyme Escherichia coli

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information second step in de novo purine biosynthesis pathway Escherichia coli ?
-
 ?

Temperature Range [°C]

Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
18
-
 no detectable activity at this temperature Escherichia coli