RGD Reference Report - Characterization of the metal-binding site in aminopeptidase B. - Rat Genome Database

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Characterization of the metal-binding site in aminopeptidase B.

Authors: Hirose, J  Ohsaki, T  Nishimoto, N  Matuoka, S  Hiromoto, T  Yoshida, T  Minoura, T  Iwamoto, H  Fukasawa, KM 
Citation: Hirose J, etal., Biol Pharm Bull. 2006 Dec;29(12):2378-82.
RGD ID: 2325932
Pubmed: PMID:17142967   (View Abstract at PubMed)

A recombinant rat aminopeptidase-B (Ap-B) was expressed as a glutathione S-transferase (GST) fusion protein in Escherichia coli BL21 harboring a plasmid pGEX-Ap-B and was purified by glutathione-Sepharose 4B and Q-Sepharose columns. The metal-substituted derivatives of Ap-B, Co(II)- and Cu(II)-Ap-B contain almost 1 mole of cobalt(II) and copper(II) ions per enzyme molecule, respectively. The specific activity of Co(II)-Ap-B is very similar to that of recombinant Ap-B but that of Cu(II)-Ap-B is very low. The dissociation constants of the zinc ions of recombinant Ap-B and of the cobalt ions of Co(II)-Ap-B calculated from the relationships between the free metal ions and the residual enzyme activities are 3.7(+/-1.0)x10(-13) and 4.7(+/-1.0)x10(-12) M, respectively. The EPR parameters (gperpendicular), g// and A//) of Cu(II)-Ap-B were 2.06, 2.27, and 156x10(-4) cm-1. The A// value and the g// of Cu(II)-Ap-B are very similar to those of Cu(II)-thermolysin or Cu(II)-dipeptidyl peptidase III, in which the coordination geometry is a distorted tetrahedral.

Gene Ontology Annotations    Click to see Annotation Detail View

Molecular Function
TermQualifierEvidenceWithReferenceNotesSourceOriginal Reference(s)
cobalt ion binding  IDA 2325932 RGD 
copper ion binding  IDA 2325932 RGD 
metalloaminopeptidase activity  IDA 2325932 RGD 
zinc ion binding  IDA 2325932 RGD 

Objects Annotated

Genes (Rattus norvegicus)
Rnpep  (arginyl aminopeptidase)


Additional Information