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Literature summary for 4.1.1.19 extracted from

  • Shah, R.; Akella, R.; Goldsmith, E.J.; Phillips, M.A.
    X-ray structure of Paramecium bursaria Chlorella virus arginine decarboxylase: insight into the structural basis for substrate specificity (2007), Biochemistry, 46, 2831-2841.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
expression of His6-tagged wild-type and mutant enzymes in Escherichia coli strain BL21(DE3) Paramecium bursaria chlorella virus

Crystallization (Commentary)

Crystallization (Comment) Organism
purified recombinant His6-tagged wild-type and mutant enzymes, 0.005 ml of 20 mg/ml protein in 10 mM HEPES, pH 7.2, 50 mM NaCl, 1 mM DTT, 0.5 mM EDTA, pH 8.0, and 0.03% v/v Brij-35, with or without 5 mM agmatine, are mixed with an equal volume of the crystallization solution containing 6% PEG 8000, 100 mM imidazole, pH 7.5, 200 mM calcium acetate, sitting drop vapour diffusion, 16°C, crystals generally grow within 24 h, cryoprotection with a solution containing the mother liquor and 25-30% 2-methyl-2,4-pentanediol, X-ray diffraction structure determination and analysis at 1.95 A and 1.8 A resolution for the free and agmatine-bound enzyme, molecular modeling Paramecium bursaria chlorella virus

Protein Variants

Protein Variants Comment Organism
T142A site-directed mutagenesis, structural comparison to the wild-type enzyme, overview Paramecium bursaria chlorella virus

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
L-arginine Paramecium bursaria chlorella virus
-
agmatine + CO2
-
?

Organism

Organism UniProt Comment Textmining
Paramecium bursaria chlorella virus
-
-
-

Reaction

Reaction Comment Organism Reaction ID
L-arginine = agmatine + CO2 the K148-loop movement may be kinetically linked to the rate-limiting step of product release, active site structure, mechanism Paramecium bursaria chlorella virus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
L-arginine
-
Paramecium bursaria chlorella virus agmatine + CO2
-
?
L-arginine the key specificity element is the 310-helix that contains and positions substrate-binding residues such as Glu296,mechanism, the 310-helix in Chlorella virus ADC is shifted over 2 A away from the pyridoxal 5'-phosphate cofactor, the K148 loop functions as an active site lid, overview Paramecium bursaria chlorella virus agmatine + CO2
-
?

Subunits

Subunits Comment Organism
More the mobile loop, the K148-loop, is observed in a closed, substrate-bound conformation, this loop adopts different conformations throughout the catalytic cycle, overview Paramecium bursaria chlorella virus

Synonyms

Synonyms Comment Organism
ADC
-
Paramecium bursaria chlorella virus
More the enzyme belongs to the group IV of pyridoxal 5'-phosphate-dependent decarboxylases belonging to the alpha/beta barrel structural family Paramecium bursaria chlorella virus

Cofactor

Cofactor Comment Organism Structure
pyridoxal 5'-phosphate dependent on, the cofactor forms an interaction with K48 via Schiff base Paramecium bursaria chlorella virus