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3.4.16.6: carboxypeptidase D

This is an abbreviated version!
For detailed information about carboxypeptidase D, go to the full flat file.

Word Map on EC 3.4.16.6

Reaction

preferential release of a C-terminal arginine or lysine residue =

Synonyms

Carboxypeptidase D, carboxypeptidase Kex1, cereal serine carboxypeptidase II, CP-MII.1, CP-MII.2, CP-MII.3, CP-WII, CPD, CPDW-II, CPW, EC 3.4.12.1, EC 3.4.16.1, EC 3.4.21.13, gene KEX1 serine carboxypeptidase, h-TLL, Kex-1 endopeptidase, Kex-1 protease, Kex1, KEX1 carboxypeptidase, Kex1 protease, KEX1 proteinase, KEX1DELTAp, Kex1p, KexA, Saccharomyces cerevisiae KEX1 gene product, serine carboxypeptidase B-like protease, wheat carboxypeptidase II

ECTree

     3 Hydrolases
         3.4 Acting on peptide bonds (peptidases)
             3.4.16 Serine-type carboxypeptidases
                3.4.16.6 carboxypeptidase D

Cloned

Cloned on EC 3.4.16.6 - carboxypeptidase D

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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
a truncated form of Kex-1, Kex-1-C611, is constructed comprising the amino acid residues from 104-611 and lacks the transmembrane domain
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a truncated form of KexA (amino acid residues 1 to 526 of KexA), which lack the potential transmembrane region and the succeeding C-terminal sequence (amino acid residues 527 to 625 of KexA) is expressed by using a protein expression system with the pIECS3 vector and Aspergillus nidulans
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individual domains of the enzyme are expressed in insect Sf9 cells using the baculovirus expression system. Medium from domain 1B-expressing cells and domain 2-expressing cells shows substantial enzymatic activity, whereas medium from domain 1A-expressing cells is not different from cells infected with wild-type virus. The individual domains 1A, 1B, and 2 are expressed in baculovirus under the polyhedrin promoter and with the signal peptide of the rat enzyme
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into the yeast shuttle vector pVT100-ZZ
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the transthyretin-like domain belonging to the first catalytic domain of human metallocarboxypeptidase D (residues 386-460, h-TTL), is cloned into the pET-22B vector to encode a C-terminal hexahistidine fusion protein. Expression carried out in Escherichia coli
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