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Literature summary extracted from

  • Furuta, K.; Nakayama, K.; Sugimoto, Y.; Ichikawa, A.; Tanaka, S.
    Activation of histidine decarboxylase through post-translational cleavage by caspase-9 in a mouse mastocytoma P-815 (2007), J. Biol. Chem., 282, 13438-13446.
    View publication on PubMed

Activating Compound

EC Number Activating Compound Comment Organism Structure
4.1.1.22 Butyrate highly activating for the wild-type enzyme Mus musculus

Application

EC Number Application Comment Organism
3.4.22.62 medicine caspase-9 is a target for development of therapeutic approaches for histamine-related diseases Mus musculus

Cloned(Commentary)

EC Number Cloned (Comment) Organism
4.1.1.22 expression of 5'-3fold FLAG-tagged and 3'-HA-tagged enzyme in 293FT and P-815 cells using a lentiviral expression system Mus musculus

Protein Variants

EC Number Protein Variants Comment Organism
4.1.1.22 C552A site-directed mutagenesis, the mutant shows similar cleavage by caspase-9 as the wild-type enzyme Mus musculus
4.1.1.22 D517A site-directed mutagenesis, the mutant shows reduced cleavage by caspase-9 compared to the wild-type enzyme Mus musculus
4.1.1.22 D518A site-directed mutagenesis, the mutant shows reduced cleavage by caspase-9 compared to the wild-type enzyme Mus musculus
4.1.1.22 D518A/D550A/D551A site-directed mutagenesis, the mutant shows highly reduced activation by butyrate compared to the wild-type enzyme Mus musculus
4.1.1.22 D547A site-directed mutagenesis, the mutant shows reduced cleavage by caspase-9 compared to the wild-type enzyme Mus musculus
4.1.1.22 D547A/P548A/F549A site-directed mutagenesis, the mutant shows highly reduced cleavage by caspase-9 compared to the wild-type enzyme Mus musculus
4.1.1.22 D550A site-directed mutagenesis, the mutant shows reduced cleavage by caspase-9 compared to the wild-type enzyme Mus musculus
4.1.1.22 D550A/D551A site-directed mutagenesis, the mutant shows highly reduced cleavage by caspase-9 compared to the wild-type enzyme Mus musculus
4.1.1.22 D550A/D551A/C552A site-directed mutagenesis, the mutant shows highly reduced cleavage by caspase-9 compared to the wild-type enzyme Mus musculus
4.1.1.22 D551A site-directed mutagenesis, the mutant shows reduced cleavage by caspase-9 compared to the wild-type enzyme Mus musculus
4.1.1.22 F549A site-directed mutagenesis, the mutant shows reduced cleavage by caspase-9 compared to the wild-type enzyme Mus musculus
4.1.1.22 I525A site-directed mutagenesis, the mutant shows reduced cleavage by caspase-9 compared to the wild-type enzyme Mus musculus
4.1.1.22 K524A site-directed mutagenesis, the mutant shows reduced cleavage by caspase-9 compared to the wild-type enzyme Mus musculus
4.1.1.22 K527A site-directed mutagenesis, the mutant shows reduced cleavage by caspase-9 compared to the wild-type enzyme Mus musculus
4.1.1.22 additional information construction of deletion mutants with altered activation by butyrate and cleavage by caspase-9, overview Mus musculus
4.1.1.22 P519A site-directed mutagenesis, the mutant shows reduced cleavage by caspase-9 compared to the wild-type enzyme Mus musculus
4.1.1.22 P548A site-directed mutagenesis, the mutant shows reduced cleavage by caspase-9 compared to the wild-type enzyme Mus musculus
4.1.1.22 Q521A site-directed mutagenesis, the mutant shows similar cleavage by caspase-9 as the wild-type enzyme Mus musculus
4.1.1.22 R523A site-directed mutagenesis, the mutant shows reduced cleavage by caspase-9 compared to the wild-type enzyme Mus musculus
4.1.1.22 T544A/M545A/P546A site-directed mutagenesis, the mutant shows highly reduced cleavage by caspase-9 compared to the wild-type enzyme Mus musculus

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.4.22.62 benzyloxycarbonyl-Leu-Glu-His-Asp-fluoromethylketone
-
 Mus musculus

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
4.1.1.22 53000
-
 2 * 53000, SDS-PAGE, 2 * 74000, recombinant 5-3fold FLAG-tagged and 3-HA-tagged enzyme, SDS-PAGE Mus musculus
4.1.1.22 74000
-
 2 * 53000, SDS-PAGE, 2 * 74000, recombinant 5-3fold FLAG-tagged and 3-HA-tagged enzyme, SDS-PAGE Mus musculus

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
3.4.22.62 L-histidine decarboxylase precursor + H2O Mus musculus in P-815 cells, histamine synthesis is augmented through the post-translational cleavage of L-histidine decarboxylase, which is mediated by caspase-9 ?
-
 ?
3.4.22.62 L-histidine decarboxylase precursor + H2O Mus musculus BDF1 in P-815 cells, histamine synthesis is augmented through the post-translational cleavage of L-histidine decarboxylase, which is mediated by caspase-9 ?
-
 ?
4.1.1.22 L-histidine Mus musculus HDC is the rate-limiting enzyme for histamine synthesis histamine + CO2
-
 ?
4.1.1.22 L-histidine Mus musculus BDF1 HDC is the rate-limiting enzyme for histamine synthesis histamine + CO2
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
3.4.22.62 Mus musculus
-
-
-
4.1.1.22 Mus musculus
-
 BDF1 mice
-
4.1.1.22 Mus musculus BDF1
-
 BDF1 mice
-

Posttranslational Modification

EC Number Posttranslational Modification Comment Organism
4.1.1.22 proteolytic modification post-translational cleavage by caspase-9 in a mouse mastocytoma P-815, residues D547-D551 and D517-K527 are important, overview Mus musculus

Source Tissue

EC Number Source Tissue Comment Organism Textmining
3.4.22.62 P-815 cell mastocytoma Mus musculus
-
4.1.1.22 mastocytoma cell
-
 Mus musculus
-
4.1.1.22 P-815 cell peritoneal cavity Mus musculus
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.4.22.62 L-histidine decarboxylase precursor + H2O
-
 Mus musculus ?
-
 ?
3.4.22.62 L-histidine decarboxylase precursor + H2O in P-815 cells, histamine synthesis is augmented through the post-translational cleavage of L-histidine decarboxylase, which is mediated by caspase-9 Mus musculus ?
-
 ?
3.4.22.62 L-histidine decarboxylase precursor + H2O
-
 Mus musculus BDF1 ?
-
 ?
3.4.22.62 L-histidine decarboxylase precursor + H2O in P-815 cells, histamine synthesis is augmented through the post-translational cleavage of L-histidine decarboxylase, which is mediated by caspase-9 Mus musculus BDF1 ?
-
 ?
4.1.1.22 L-histidine
-
 Mus musculus histamine + CO2
-
 ?
4.1.1.22 L-histidine HDC is the rate-limiting enzyme for histamine synthesis Mus musculus histamine + CO2
-
 ?
4.1.1.22 L-histidine
-
 Mus musculus BDF1 histamine + CO2
-
 ?
4.1.1.22 L-histidine HDC is the rate-limiting enzyme for histamine synthesis Mus musculus BDF1 histamine + CO2
-
 ?

Subunits

EC Number Subunits Comment Organism
4.1.1.22 dimer 2 * 53000, SDS-PAGE, 2 * 74000, recombinant 5'-3fold FLAG-tagged and 3'-HA-tagged enzyme, SDS-PAGE Mus musculus

Synonyms

EC Number Synonyms Comment Organism
4.1.1.22 HDC
-
 Mus musculus

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
4.1.1.22 37
-
 assay at Mus musculus

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
4.1.1.22 6.8
-
 assay at Mus musculus

Cofactor

EC Number Cofactor Comment Organism Structure
4.1.1.22 pyridoxal 5'-phosphate
-
 Mus musculus