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Literature summary for 6.1.1.21 extracted from

  • Levine, S.M.; Raben, N.; Xie, D.; Askin, F.B.; Tuder, R.; Mullins, M.; Rosen, A.; Casciola-Rosen, L.A.
    Novel conformation of histidyl-transfer RNA synthetase in the lung: the target tissue in Jo-1 autoantibody-associated myositis (2007), Arthritis Rheum., 56, 2729-2739.
    View publication on PubMed

Protein Variants

Protein Variants Comment Organism
D48A site-directed mutagenesis, the mutant is cleaved by caspase-6, but not by granzyme B Homo sapiens
additional information HisRS granzyme B site mapping using site-directed mutagenesis 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 + L-histidine + tRNAHis Homo sapiens strong association of autoantibodies, specificity recognizing the enzyme's granzyme B binding site of the lung enzyme, to HisRS with interstitial lung disease in patients with myositis AMP + diphosphate + L-histidinyl-tRNAHis
-
?

Organism

Organism UniProt Comment Textmining
Homo sapiens
-
Jo-1-positive patients with myositis
-

Posttranslational Modification

Posttranslational Modification Comment Organism
proteolytic modification lung HisRS cleavage by the cytotoxic lymphocyte serine protease granzyme B in vitro at LGPD48, caspase 6, which shares a tetrapeptide specificity similar to that of granzyme B, cleaves HisRS, producing a fragment of similar size, but cleavage sites are nonoverlapping Homo sapiens

Source Tissue

Source Tissue Comment Organism Textmining
lung
-
Homo sapiens
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + L-histidine + tRNAHis
-
Homo sapiens AMP + diphosphate + L-histidinyl-tRNAHis
-
?
ATP + L-histidine + tRNAHis strong association of autoantibodies, specificity recognizing the enzyme's granzyme B binding site of the lung enzyme, to HisRS with interstitial lung disease in patients with myositis Homo sapiens AMP + diphosphate + L-histidinyl-tRNAHis
-
?

Synonyms

Synonyms Comment Organism
HisRS
-
Homo sapiens
histidyl-transfer RNA synthetase
-
Homo sapiens
Jo-1
-
Homo sapiens

Cofactor

Cofactor Comment Organism Structure
ATP
-
Homo sapiens