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Literature summary extracted from

  • Sparla, F.; Costa, A.; Lo Schiavo, F.; Pupillo, P.; Trost, P.
    Redox regulation of a novel plastid-targeted beta-amylase of Arabidopsis (2006), Plant Physiol., 141, 840-850.
    View publication on PubMedView publication on EuropePMC

Activating Compound

EC Number Activating Compound Comment Organism Structure
3.2.1.2 additional information the enzyme requires reducing conditions for full activity Arabidopsis thaliana
3.2.1.2 reduced DTT strong activation of isozyme TR-BAMY Arabidopsis thaliana
3.2.1.2 thioredoxin thioredocins f1, m1, and y1, the isozyme TR-BAMY is positively thioredoxin-regulated Arabidopsis thaliana

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.2.1.2 isozyme CT-BAMY, DNA and amino acid sequence determination and analysis Arabidopsis thaliana
3.2.1.2 isozyme TR-BAMY, DNA and amino acid sequence determination and analysis, functional expression of mature isozyme TR-BAMY and of mutant enzymes in Escherichia coli strains HB101 and BL21(DE3), transient expression of GFP-tagged isozyme TR-BAMY in Nicotiana tabacum protoplasts with exclusive association to the chloroplasts Arabidopsis thaliana

Protein Variants

EC Number Protein Variants Comment Organism
3.2.1.2 C148S site-directed mutagenesis, the mutant shows a redox sensitivity similar to the wild-type enzyme Arabidopsis thaliana
3.2.1.2 C206S site-directed mutagenesis, the mutant shows a redox sensitivity similar to the wild-type enzyme Arabidopsis thaliana
3.2.1.2 C261S site-directed mutagenesis, the mutant shows a redox sensitivity similar to the wild-type enzyme Arabidopsis thaliana
3.2.1.2 C32S site-directed mutagenesis, the mutant shows 70% impaired redox sensitivity compared to the wild-type enzyme Arabidopsis thaliana
3.2.1.2 C399S site-directed mutagenesis, the mutant shows a redox sensitivity similar to the wild-type enzyme Arabidopsis thaliana
3.2.1.2 C413S site-directed mutagenesis, the mutant shows a redox sensitivity similar to the wild-type enzyme Arabidopsis thaliana
3.2.1.2 C470S site-directed mutagenesis, the mutant shows 70% impaired redox sensitivity compared to the wild-type enzyme Arabidopsis thaliana
3.2.1.2 C506S site-directed mutagenesis, the mutant shows a redox sensitivity similar to the wild-type enzyme Arabidopsis thaliana

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.2.1.2 additional information the 41 amino acid transit peptide inhibits isozyme TR-BAMY Arabidopsis thaliana

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
3.2.1.2 chloroplast plastid-targeted isozyme CT-BAMY, contains a plastid transit peptide Arabidopsis thaliana 9507
-
3.2.1.2 chloroplast plastid-targeted isozyme TR-BAMY, contains a plastid transit peptide of 41 amino acids Arabidopsis thaliana 9507
-
3.2.1.2 plastid plastid-targeted isozyme TR-BAMY, contains a plastid transit peptide of 41 amino acids Arabidopsis thaliana 9536
-

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
3.2.1.2 60000
-
 recombinant mature isozyme TR-BAMY, gel filtration Arabidopsis thaliana
3.2.1.2 64000
-
 recombinant precursor isozyme TR-BAMY, gel filtration Arabidopsis thaliana

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
3.2.1.2 additional information Arabidopsis thaliana the isozyme TR-BAMY is redox- and thioredoxin-regulated involving residues C470 and C32 forming a disulfide bridge, the precursor enzyme conatining the transit pepetide is inactive ?
-
 ?
3.2.1.2 starch + H2O Arabidopsis thaliana
-
 maltose + ?
-
 ?
3.2.1.2 starch + H2O Arabidopsis thaliana the isozyme is involved in leaf starch degradation maltose + ?
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
3.2.1.2 Arabidopsis thaliana O23553 gene At4g170990, isozyme CT-BAMY; contains six extrachlorplastic isozymes, and three plastid-targeted isozymes
-
3.2.1.2 Arabidopsis thaliana Q9LIR6 gene At3g23920/F14O13_11, isozyme TR-BAMY; contains six extrachloroplastic isozymes, and three plastid-targeted isozymes
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.2.1.2 native isozyme partially by chloroplast purification Arabidopsis thaliana
3.2.1.2 native isozyme partially by chloroplast purification, recombinant mature isozyme TR-BAMY and recombinant mutant enzymes from Escherichia coli Arabidopsis thaliana

Source Tissue

EC Number Source Tissue Comment Organism Textmining
3.2.1.2 flower isozyme TR-BAMY Arabidopsis thaliana
-
3.2.1.2 leaf isozyme TR-BAMY Arabidopsis thaliana
-
3.2.1.2 pollen isozyme TR-BAMY Arabidopsis thaliana
-
3.2.1.2 root isozyme TR-BAMY Arabidopsis thaliana
-
3.2.1.2 seed isozyme TR-BAMY Arabidopsis thaliana
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.2.1.2 4-nitrophenyl maltopentaose + H2O
-
 Arabidopsis thaliana 4-nitrophenol + maltopentaose
-
 ?
3.2.1.2 additional information the isozyme TR-BAMY is redox- and thioredoxin-regulated involving residues C470 and C32 forming a disulfide bridge, the precursor enzyme conatining the transit pepetide is inactive Arabidopsis thaliana ?
-
 ?
3.2.1.2 starch + H2O
-
 Arabidopsis thaliana maltose + ?
-
 ?
3.2.1.2 starch + H2O soluble starch Arabidopsis thaliana maltose + ?
-
 ?
3.2.1.2 starch + H2O the isozyme is involved in leaf starch degradation Arabidopsis thaliana maltose + ?
-
 ?

Subunits

EC Number Subunits Comment Organism
3.2.1.2 monomer 1 * 60000, recombinant mature isozyme TR-BAMY, SDS-PAGE, 1 * 64000, recombinant precursor isozyme TR-BAMY, SDS-PAGE Arabidopsis thaliana

Synonyms

EC Number Synonyms Comment Organism
3.2.1.2 CT-BMY
-
 Arabidopsis thaliana
3.2.1.2 TR-BAMY
-
 Arabidopsis thaliana

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.2.1.2 37
-
 assay at Arabidopsis thaliana

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.2.1.2 additional information
-
 the isozyme TR-BAMY shifts between an active and an inactive form dependent on the pH Arabidopsis thaliana
3.2.1.2 6 8
-
 Arabidopsis thaliana