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Literature summary for 4.1.1.19 extracted from

  • Counts, K.G.; Wong, I.; Oliveira, M.A.
    Investigating the geminal diamine intermediate of Yersinia pestis arginine decarboxylase with substrate, product, and inhibitors using single wavelength stopped-flow spectroscopy (2007), Biochemistry, 46, 379-386.
    View publication on PubMed
Search for more literature for 4.1.1.19

Application

Application Comment Organism
drug development the enzyme is an attractive target for drug design Yersinia pestis

Cloned(Commentary)

Cloned (Comment) Organism
gene speA, expression of His-tagged enzyme in Escherichia coli Yersinia pestis

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
 additional information pre-steady-state kinetics of substrate, product, and inhibitor with ADC by single-wavelength stopped-flow spectroscopy, overview Yersinia pestis

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ required for activity Yersinia pestis

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
L-arginine Yersinia pestis ADC is the primary polyamine biosynthetic enzyme in the pathway agmatine + CO2
-
 ?

Organism

Organism UniProt Comment Textmining
Yersinia pestis Q8ZHG8 gene speA
-

Purification (Commentary)

Purification (Comment) Organism
recombinant His-tagged enzyme from Escherichia coli by nickel affinity chromatography Yersinia pestis

Reaction

Reaction Comment Organism Reaction ID
L-arginine = agmatine + CO2 reaction mechanism via geminal diamine intermediate Yersinia pestis
a

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
L-arginine ADC is the primary polyamine biosynthetic enzyme in the pathway Yersinia pestis agmatine + CO2
-
 ?
L-arginine the enzyme exists in two different conformational states, one that binds ligand and one that does not Yersinia pestis agmatine + CO2
-
 ?

Subunits

Subunits Comment Organism
More the enzyme exists in two different conformational states, one that binds ligand and one that does not, overview Yersinia pestis

Synonyms

Synonyms Comment Organism
ADC
-
 Yersinia pestis

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.5
-
 assay at Yersinia pestis

Cofactor

Cofactor Comment Organism Structure
pyridoxal 5'-phosphate a fold III, pyridoxal 5'-phosphate-dependent enzyme Yersinia pestis