Literature summary for 3.4.24.21 extracted from
Sarkar, I.
To compare the active sites of a series of astacin family proteases by multiple sequence alignment and homology modelling methods (2015), Comput. Adv. Commun. Circ. Syst.: ICCACCS 2014, 335, 145-150 .
No PubMed abstract available
Cloned(Commentary)
Cloned (Comment) |
Organism |
gene BMP1, sequence comparison with meprin A (EC 3.4.24.18) and meprin B (EC 3.4.24.63) of the astacin enzyme family |
Homo sapiens |
Inhibitors
Inhibitors |
Comment |
Organism |
Structure |
additional information |
inhibitor coordinates the catalytic zinc ion via carbonyl oxygen of glycine and O atom of hydroxamic acid |
Homo sapiens |
|
Metals/Ions
Metals/Ions |
Comment |
Organism |
Structure |
additional information |
inhibitor coordinates the catalytic zinc ion via carbonyl oxygen of glycine and O atom of hydroxamic acid |
Homo sapiens |
|
Zn2+ |
a zinc metalloproteinase, catalytic zinc ion |
Homo sapiens |
|
Organism
Organism |
UniProt |
Comment |
Textmining |
Homo sapiens |
P13497 |
- |
- |
Synonyms
Synonyms |
Comment |
Organism |
BMP-1 |
- |
Homo sapiens |
bone morphogenetic protein 1 |
- |
Homo sapiens |
General Information
General Information |
Comment |
Organism |
evolution |
the enzyme belongs to the astacin family of zinc-dependent endopeptidase. All the members of this family have a protease domain containing approximately 200 amino acids, which shares an amino-acid sequence similarity of 29-99%. Astacin family members are characterized by a unique 18 amino acid signature sequence HEXXHXXGFXHEXXRXDR containing the Zn binding motif HEXXH present in all metalloendopeptidases. Most of the known family members contain a COOH terminal to the protease domain. They are found to contain one or more copies of the EGF (epidermal growth factor) like E and/or CUB (complement subcomponents) domain. Differences in the active sites and inhibitor sites of astacin/BMP1, human meprin alpha, and human meprin beta, overview. The subsites S1, S2, S3, S1', S2', S3' have differences in amino acid residues. Structure homology modelling |
Homo sapiens |