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Literature summary for 3.4.24.19 extracted from

  • Chaudhuri, A.; Chakraborty, S.
    Structure-activity relationship of astacin metalloproteases A comparative study using EDTA (2018), Curr. Enzyme Inhib., 14, 131-140 .
No PubMed abstract available
Search for more literature for 3.4.24.19

Cloned(Commentary)

Cloned (Comment) Organism
gene dtld, sequence comparisons Drosophila melanogaster
gene mbmp1, sequence comparisons Mus musculus
gene Xebmp1, sequence comparisons Xenopus laevis

Inhibitors

Inhibitors Comment Organism Structure
EDTA a common inhibitor of several astacin metalloproteases Drosophila melanogaster
EDTA a common inhibitor of several astacin metalloproteases Mus musculus
EDTA a common inhibitor of several astacin metalloproteases Xenopus laevis

Localization

Localization Comment Organism GeneOntology No. Textmining
extracellular
-
 Mus musculus
-
-
extracellular
-
 Xenopus laevis
-
-
extracellular
-
 Drosophila melanogaster
-
-

Metals/Ions

Metals/Ions Comment Organism Structure
Zn2+ zinc metalloproteinase Mus musculus
Zn2+ zinc metalloproteinase Xenopus laevis
Zn2+ zinc metalloproteinase Drosophila melanogaster

Organism

Organism UniProt Comment Textmining
Drosophila melanogaster P25723
-
-
Mus musculus P98063
-
-
Xenopus laevis P98070
-
-

Synonyms

Synonyms Comment Organism
BMP-1
-
 Mus musculus
BMP-1
-
 Xenopus laevis
bone morphogenetic protein 1
-
 Mus musculus
bone morphogenetic protein 1
-
 Xenopus laevis
dorsal-ventral patterning protein tolloid
-
 Drosophila melanogaster
Tld
-
 Drosophila melanogaster

General Information

General Information Comment Organism
evolution the enzyme encoded by bmp1 belongs to the BTP cluster of the astacin enzyme family. Structure-activity relationship of astacin metalloproteases, EDTA is used to dock into the active site cleft of the astacins to know the interaction network and to identify the important residues for binding, comparative three-dimensional structure homology modeling (template crystal structure PDB ID 3EDH) and docking study, and potential binding site, detailed overview Xenopus laevis
evolution the enzyme encoded by bmp1 belongs to the BTP cluster of the astacin enzyme family. Structure-activity relationship of astacin metalloproteases, EDTA is used to dock into the active site cleft of the astacins to know the interaction network and to identify the important residues for binding, comparative three-dimensional structure homology modeling and docking study, and potential binding site, detailed overview Mus musculus
evolution the enzyme encoded by tld belongs to the BTP cluster of the astacin enzyme family. Structure-activity relationship of astacin metalloproteases, EDTA is used to dock into the active site cleft of the astacins to know the interaction network and to identify the important residues for binding, comparative three-dimensional structure homology modeling and docking study, and potential binding site, detailed overview Drosophila melanogaster
additional information the hydrogen bonding residue of the enzyme is Glu219, comparative three-dimensional structure homology modeling (template crystal structure PDB ID 3EDH) and docking study, and potential binding site, detailed overview Mus musculus
additional information the hydrogen bonding residues of the enzyme are Glu232, Ser294, and Tyr290, comparative three-dimensional structure homology modeling (template crystal structure PDB ID 3EDH) and docking study, and potential binding site, detailed overview Drosophila melanogaster
additional information the hydrogen bonding residues of the enzyme are Ser163, Tyr235, and Arg265, comparative three-dimensional structure homology modeling and docking study, and potential binding site, detailed overview Xenopus laevis