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Literature summary for 6.1.1.21 extracted from

  • Li, L.; Weinreb, V.; Francklyn, C.; Carter, C.W.
    Histidyl-tRNA synthetase urzymes: class I and II aminoacyl tRNA synthetase urzymes have comparable catalytic activities for cognate amino acid activation (2011), J. Biol. Chem., 286, 10387-10395.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 6.1.1.21

Cloned(Commentary)

Cloned (Comment) Organism
gene hisS, expression of HisRS active site fragments, HisRS1-HisRS4, as maltose-binding proteins fusion proteins in Escherichia coli strain BL21(DE3)pLysS Escherichia coli

Protein Variants

Protein Variants Comment Organism
additional information construction of four minimal, active site fragments, urzymes, of Escherichia coli class II HisRS by PCR-based subcloning, the fragments comprise: HisRS1 residues 16-134, HisRS2 residues 10-134, HisRS3 residues 16-134 and 301-320, and HisRS4 residues 10-134 and 301-320. HisRS-3 binds ATP far more tightly and histidine less strongly than native, full-length HisRS or its intact catalytic domain. HisRS-3 urzyme steady-state kinetic parameters differ substantially from those of native full-length HisRS. All urzymes show relative rate enhancements compared to the wild-type enzyme, overview Escherichia coli

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
 additional information Michaelis-Menten kinetics for the wild-type enzyme and recombinant HisRS active site fragments, HisRS1-HisRS4, overview Escherichia coli

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ required Escherichia coli

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
ATP + L-histidine + tRNAHis Escherichia coli
-
 AMP + diphosphate + L-histidyl-tRNAHis
-
 ?

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
 gene hisS
-

Purification (Commentary)

Purification (Comment) Organism
recombinant maltose-binding fusion HisRS active site fragments, HisRS1-HisRS4, from Escherichia coli strain BL21(DE3)pLysS by amylose affinity chromatography, fusion protein cleavage by TEV. The fusion protein does not affect urzyme activity Escherichia coli

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + L-histidine + tRNAHis
-
 Escherichia coli AMP + diphosphate + L-histidyl-tRNAHis
-
 ?

Synonyms

Synonyms Comment Organism
class II histidyl-tRNA synthetase
-
 Escherichia coli
HisRS
-
 Escherichia coli
HisRS-1
-
 Escherichia coli
HisRS-2
-
 Escherichia coli
Histidyl-tRNA synthetase
-
 Escherichia coli

Cofactor

Cofactor Comment Organism Structure
ATP
-
 Escherichia coli

General Information

General Information Comment Organism
evolution significantly different rate enhancements by four HisRS urzymes demonstrate that amino acid activation provides an experimental metric for recapitulating very early evolutionary events. Catalytic activities of HisRS-1 and HisRS-2 provide complementary support for Rodin-Ohno hypothesis that ancestral class I and II aaRS were encoded on opposite strands of same gene Escherichia coli