Poly(3-hydroxybutyrate) depolymerases bind to their substrate by a C-terminal located substrate binding site
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چکیده
منابع مشابه
The substrate binding site of pepsin.
In earlier reports from this laboratory, a series of new synthetic substrates for pepsin was described.'-' These compounds are of the general type Z-His-X-YOAI\e4 where X and Y are the residues of amino acids such as L-phenylalanine, p-nitro-L-phenylalanine, L-tyrosine, L-tryptophan, and L-leucine; the enzymic action is limited to the cleavage of the X-Y bond. One of the substrate analogues pre...
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To investigate the role of each domain in BiP/GRP78 function, we have used a full-length recombinant BiP engineered to contain two enterokinase sites; one site is located after an N-terminal FLAG epitope, and a second site has been inserted at the junction between the N- and C-terminal domains (FLAG-BiP.ent). FLAG-BiP.ent oligomerizes into multiple species that interconvert with each other in a...
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BACKGROUND Archaemetzincins are metalloproteases occurring in archaea and some mammalia. They are distinct from all the other metzincins by their extended active site consensus sequence HEXXHXXGXXHCX(4)CXMX(17)CXXC featuring four conserved cysteine residues. Very little is known about their biological importance and structure-function relationships. PRINCIPAL FINDINGS Here we present three cr...
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in cell-substratum contact sites. homologous to a v-src substrate and is located overexpressed in human carcinomas, is The product of the EMS1 gene, amplified and
متن کاملDetermination of the substrate-docking site of protein tyrosine kinase C-terminal Src kinase.
Protein tyrosine kinases (PTK) are key enzymes of mammalian signal transduction. For the fidelity of signal transduction, each PTK phosphorylates only one or a few proteins on specific Tyr residues. Substrate specificity is thought to be mediated by PTK-substrate docking interactions and recognition of the phosphorylation site sequence by the kinase active site. However, a substrate-docking sit...
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ژورنال
عنوان ژورنال: FEMS Microbiology Letters
سال: 1996
ISSN: 0378-1097
DOI: 10.1016/0378-1097(96)00305-9