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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