Characterization of residues involved in the activity and degradation of histidine decarboxylase by site-directed mutagenesis

Project Information

Grant agreement ID: FMBI950001

Project closed

Start date 22 May 1996

End date 21 May 1997

Funded under

• Specific research and technological development programme in the field of the training and mobility of researchers, 1994-1998

Total cost No data

EU contribution No data

Coordinated by

Universidad de Málaga
Spain

Objective

Mammalian L-amino acid decarboxylases producing 1,4-diamines: histidine decarboxylase (HDC), aromatic L-amino acid decarboxylase (DDC) and ornithine decarboxylase (ODC); and their products: histamine, serotonin, tryptamine and putrescine, exhibit functional, metabolic and enzymic properties in common. HDC has been related to very different topics: alergy, neurochemistry and cell proliferation, as also described for DD and ODC. The Host Group have detected some analogies among the deduced primary sequences of these proteins. The common protein motifs observed every mammalian L-amino acid decarboxylase could be involved in the rapid turnover of these enzymes and/or in the decarboxylation mechanisms. In order to check this hypothesis, we will study the post-translational modifications and activities of expressed recombinant cDNAs encoding the rat mature HDC subunit and directed mutant DNA sequences. The characterization of the molecular underlying mechanisms of L-amino acid decarboxylase turnover and catalysis mechanisms will provide important basis for therapeutic strategies in alergy, neurochemistry and cell proliferation fields.

Fields of science (EuroSciVoc)

CORDIS classifies projects with EuroSciVoc, a multilingual taxonomy of fields of science, through a semi-automatic process based on NLP techniques. See: https://op.europa.eu/en/web/eu-vocabularies/euroscivoc.

• natural sciences › biological sciences › genetics › DNA
• natural sciences › chemical sciences › catalysis
• natural sciences › biological sciences › biochemistry › biomolecules › proteins › enzymes

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Programme(s)

• FP4-TMR - Specific research and technological development programme in the field of the training and mobility of researchers, 1994-1998

Topic(s)

• 0302 - Post-doctoral research training grants
• TL02 - Molecular Biology and Biochemistry

Call for proposal

Data not available

Funding Scheme

RGI - Research grants (individual fellowships)

Coordinator

Universidad de Málaga

• EU contribution: No data
• Address: S/N,Campus de Teatinos ; 29071 Málaga ; Spain
• Total cost: No data

Participants (1)

Not available

Spain

• EU contribution: No data
• Total cost: No data