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Literature summary for 6.1.1.14 extracted from

  • Surguchov, A.P.; Surguchova, I.G.
    Two enzymatically active forms of glycyl-tRNA synthetase from Bacillus brevis (1975), Eur. J. Biochem., 54, 175-184.
    View publication on PubMed
Search for more literature for 6.1.1.14

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
30000
-
 2 * 30000 (alpha) + 2 * 81000 (beta), enzyme form E1, SDS-PAGE, 2 * 30000, SDS-PAGE, enzyme form E2, E2 is a component of E1, SDS-PAGE Brevibacillus brevis
66000
-
 gel filtration, enzyme form E2 Brevibacillus brevis
81000
-
 2 * 30000 (alpha) + 2 * 81000 (beta), enzyme form E1, SDS-PAGE, 2 * 30000, SDS-PAGE, enzyme form E2, E2 is a component of E1, SDS-PAGE Brevibacillus brevis
226000
-
 gel filtration, enzyme form E1 Brevibacillus brevis

Organism

Organism UniProt Comment Textmining
Brevibacillus brevis
-
-
-

Purification (Commentary)

Purification (Comment) Organism
2 enzyme forms: E1 and E2 Brevibacillus brevis

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
additional information
-
-
 Brevibacillus brevis

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + glycine + tRNAGly
-
 Brevibacillus brevis AMP + diphosphate + glycyl-tRNAGly
-
 ?
additional information formation of glycine hydroxamate Brevibacillus brevis ?
-
 ?
additional information catalyzes glycine-dependent ATP-diphosphate exchange Brevibacillus brevis ?
-
 ?

Subunits

Subunits Comment Organism
tetramer 2 * 30000 (alpha) + 2 * 81000 (beta), enzyme form E1, SDS-PAGE, 2 * 30000, SDS-PAGE, enzyme form E2, E2 is a component of E1, SDS-PAGE Brevibacillus brevis