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Literature summary for 6.1.1.14 extracted from

  • Xie, W.; Nangle, L.A.; Zhang, W.; Schimmel, P.; Yang, X.L.
    Long-range structural effects of a Charcot-Marie-Tooth disease-causing mutation in human glycyl-tRNA synthetase (2007), Proc. Natl. Acad. Sci. USA, 104, 9976-9981.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 6.1.1.14

Protein Variants

Protein Variants Comment Organism
G526R naturally occuring mutation at the site for synthesis of glycyl-adenylate, G526 is a strictly conserved residue in the middle of motif 3, the mutant is inactive and shows tighter dimer interaction compared to the wild-type enzyme, long-range structural effects of the Charcot-Marie-Tooth disease-causing mutation in the human enzyme, overview Homo sapiens

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+
-
 Homo sapiens

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
ATP + glycine + tRNAGly Homo sapiens GlyRS mutations cause Charcot-Marie-Tooth peripheral neuropathies, the most common heritable disease of the peripheral nervous system, overview AMP + diphosphate + glycyl-tRNAGly
-
 ?

Organism

Organism UniProt Comment Textmining
Homo sapiens P41250
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + glycine + tRNAGly two-step reaction Homo sapiens AMP + diphosphate + glycyl-tRNAGly
-
 ?
ATP + glycine + tRNAGly GlyRS mutations cause Charcot-Marie-Tooth peripheral neuropathies, the most common heritable disease of the peripheral nervous system, overview Homo sapiens AMP + diphosphate + glycyl-tRNAGly
-
 ?

Subunits

Subunits Comment Organism
dimer homodimer, crystal structure, overall structural organization of GlyRS, overview Homo sapiens
More structural alignment with the GlyRS from Thermus thermophilus Homo sapiens

Synonyms

Synonyms Comment Organism
Glycyl-tRNA synthetase
-
 Homo sapiens
GlyRS
-
 Homo sapiens

Cofactor

Cofactor Comment Organism Structure
ATP
-
 Homo sapiens