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Literature summary for 4.1.1.11 extracted from

  • Gopalan, G.; Chopra, S.; Ranganathan, A.; Swaminathan, K.
    Crystal structure of uncleaved L-aspartate-alpha-decarboxylase from Mycobacterium tuberculosis (2006), Proteins, 65, 796-802.
    View publication on PubMed
Search for more literature for 4.1.1.11

Application

Application Comment Organism
drug development the enzyme is a target for structure-based drug development Mycobacterium tuberculosis

Cloned(Commentary)

Cloned (Comment) Organism
ADC expression analysis, expression of the HIs-tagged enzyme in Escherichia coli Mycobacterium tuberculosis

Crystallization (Commentary)

Crystallization (Comment) Organism
purified recombinant His-tagged unprocessed, native precursor ADC, vapor diffusion hanging drop method, the precipitant solution contains 0.1 M sodium cacodylate, pH 6.5, 1.5 M magnesium sulfate, and 20% w/v PEG 2000, 15 days, cryoprotection by 20% v/v glycerol, X-ray diffraction structure determination and analysis at 2.99 A resolution Mycobacterium tuberculosis

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
L-aspartate Mycobacterium tuberculosis the enzyme is a critical regulatory enzyme in the pantothenate biosynthetic pathway beta-alanine + CO2
-
 ?

Organism

Organism UniProt Comment Textmining
Mycobacterium tuberculosis
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-
-

Posttranslational Modification

Posttranslational Modification Comment Organism
proteolytic modification the enzyme is autocatalytically self-processing, overview Mycobacterium tuberculosis

Purification (Commentary)

Purification (Comment) Organism
recombinant His-tagged enzyme from Escherichia coli by nickel affinity chromatography and gel filtration Mycobacterium tuberculosis

Source Tissue

Source Tissue Comment Organism Textmining
additional information enzyme expression analysis Mycobacterium tuberculosis
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
L-aspartate the enzyme is a critical regulatory enzyme in the pantothenate biosynthetic pathway Mycobacterium tuberculosis beta-alanine + CO2
-
 ?
L-aspartate Ser25 is the catalytic residue, self-processing and catalytic mechanism, overview Mycobacterium tuberculosis beta-alanine + CO2
-
 ?

Subunits

Subunits Comment Organism
octamer two tetramers forming a pseudo fourfold rotational symmetry, the enzyme protein shows a double-psi beta-barrel structure Mycobacterium tuberculosis

Synonyms

Synonyms Comment Organism
ADC
-
 Mycobacterium tuberculosis
L-Aspartate-alpha-decarboxylase
-
 Mycobacterium tuberculosis
More the enzyme belongs to a small class of self-cleaving and pyruvoyl-dependent amino acid decarboxylases Mycobacterium tuberculosis