Literature summary for 4.1.1.22 extracted from

Fleming, J.V.; Fajardo, I.; Langlois, M.R.; Sanchez-Jimenez, F.; Wang, T.C.
The C-terminus of rat L-histidine decarboxylase specifically inhibits enzymic activity and disrupts pyridoxal phosphate-dependent interactions with L-histidine substrate analogues (2004), Biochem. J., 381, 769-778.

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Organism

Organism	UniProt	Comment	Textmining
Rattus norvegicus	-	-	-

Posttranslational Modification

Posttranslational Modification	Comment	Organism
proteolytic modification	C-terminal processing of the about 74 kDa full-length protein occurs naturally in vivo, with the production of multiple truncated isoforms. The 74 kDa full-length isoform is deficient in substrate binding, the C-terminally truncated isoforms with molecular masses between 70 kDa and 58 kDa have gradually increasing specific activities	Rattus norvegicus

Purification (Commentary)

Purification (Comment)	Organism
recombinant His-tagged enzyme	Rattus norvegicus

Source Tissue

Source Tissue	Comment	Organism	Textmining

Cofactor

Cofactor	Comment	Organism	Structure
pyridoxal 5'-phosphate	dependent on	Rattus norvegicus

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Release 2023.1 (January 2023)