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Literature summary 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

Application

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

Cloned(Commentary)

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

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
4.1.1.11 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)

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

Organism

EC Number Organism UniProt Comment Textmining
4.1.1.11 Mycobacterium tuberculosis
-
-
-

Posttranslational Modification

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

Purification (Commentary)

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

Source Tissue

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

Substrates and Products (Substrate)

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

Subunits

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

Synonyms

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