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Literature summary for 4.1.1.22 extracted from

  • Fennell, L.M.; Fleming, J.V.
    Differential processing of mammalian L-histidine decarboxylase enzymes (2014), Biochem. Biophys. Res. Commun., 445, 304-309.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
expression in COS7 cell Homo sapiens
expression in COS7 cell Rattus norvegicus

Protein Variants

Protein Variants Comment Organism
D543A/D544A mutation in conserved di-aspartate motif. Mutation does not lead to a loss in levels of any of the processed isoforms Rattus norvegicus
D551A/D552A mutation in conserved di-aspartate motif. Mutation does not lead to a loss in levels of any of the processed isoforms Homo sapiens
DD513A/D514A mutation in conserved di-aspartate motif. Mutation does not lead to a loss in levels of any of the processed isoforms Homo sapiens
DD519A/D520A mutation in conserved di-aspartate motif. Mutation does not lead to a loss in levels of any of the processed isoforms Rattus norvegicus
additional information mutation of an EEAPD motif at amino acids 556-560 of the human hHDC protein leads to a decrease in the 59 kDa processed band Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens
-
-
-
Rattus norvegicus
-
-
-

Posttranslational Modification

Posttranslational Modification Comment Organism
proteolytic modification enzyme undergoes processing with a major processed band of 59 kDa being observed in addition to a number of minor bands. Processing to the 59 kDa band is caspase-6 dependent Homo sapiens
proteolytic modification the protein is processed into major 63, 54 and 58/59 kDa doublet bands. Processing at the HDC SKD 501/502/503 site is likely to be caspase-dependent Rattus norvegicus

Source Tissue

Source Tissue Comment Organism Textmining
testis
-
Homo sapiens
-