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Literature summary for 3.4.24.18 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 3.4.24.18

Cloned(Commentary)

Cloned (Comment) Organism
gene Mep1A, sequence comparisons Mus musculus
gene Mep1A, sequence comparisons Rattus norvegicus

Inhibitors

Inhibitors Comment Organism Structure
EDTA a common inhibitor of several astacin metalloproteases Mus musculus
EDTA a common inhibitor of several astacin metalloproteases Rattus norvegicus

Localization

Localization Comment Organism GeneOntology No. Textmining
extracellular
-
 Mus musculus
-
-
extracellular
-
 Rattus norvegicus
-
-

Metals/Ions

Metals/Ions Comment Organism Structure
Zn2+ zinc metalloproteinase Mus musculus
Zn2+ zinc metalloproteinase Rattus norvegicus

Organism

Organism UniProt Comment Textmining
Mus musculus P28825
-
-
Rattus norvegicus Q64230
-
-

Synonyms

Synonyms Comment Organism
MEP1A
-
 Mus musculus
MEP1A
-
 Rattus norvegicus
meprin alpha
-
 Mus musculus
meprin alpha
-
 Rattus norvegicus
Mmepa
-
 Mus musculus
Rmepa
-
 Rattus norvegicus

General Information

General Information Comment Organism
evolution the enzyme encoded by Mmepa 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 Rmepa 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 Rattus norvegicus
additional information the hydrogen bonding residues of the enzyme are Ser131, Glu157, His166, Ser169, and Tyr195, comparative three-dimensional structure homology modeling (template crystal structure PDB ID 4GWN) and docking study, and potential binding site, detailed overview Rattus norvegicus
additional information the hydrogen bonding residues of the enzyme are Thr151 and Leu210, comparative three-dimensional structure homology modeling (template crystal structure PDB ID 4GWN) and docking study, and potential binding site, detailed overview Mus musculus