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1ft7

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[[Image:1ft7.jpg|left|200px]]
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{{STRUCTURE_1ft7| PDB=1ft7 | SCENE= }}
{{STRUCTURE_1ft7| PDB=1ft7 | SCENE= }}
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'''AAP COMPLEXED WITH L-LEUCINEPHOSPHONIC ACID'''
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===AAP COMPLEXED WITH L-LEUCINEPHOSPHONIC ACID===
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==Overview==
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The nature of the interaction of the transition-state analogue inhibitor L-leucinephosphonic acid (LPA) with the leucine aminopeptidase from Aeromonas proteolytica (AAP) was investigated. LPA was shown to be a competitive inhibitor at pH 8.0 with a K(i) of 6.6 microM. Electronic absorption spectra, recorded at pH 7.5 of [CoCo(AAP)], [CoZn(AAP)], and [ZnCo(AAP)] upon addition of LPA suggest that LPA interacts with both metal ions in the dinuclear active site. EPR studies on the Co(II)-substituted forms of AAP revealed that the environments of the Co(II) ions in both [CoZn(AAP)] and [ZnCo(AAP)] become highly asymmetric and constrained upon the addition of LPA and clearly indicate that LPA interacts with both metal ions. The X-ray crystal structure of AAP complexed with LPA was determined at 2.1 A resolution. The X-ray crystallographic data indicate that LPA interacts with both metal centers in the dinuclear active site of AAP and a single oxygen atom bridge is absent. Thus, LPA binds to the dinuclear active site of AAP as an eta-1,2-mu-phosphonate with one ligand to the second metal ion provided by the N-terminal amine. A structural comparison of the binding of phosphonate-containing transition-state analogues to the mono- and bimetallic peptidases provides insight into the requirement for the second metal ion in bridged bimetallic peptidases. On the basis of the results obtained from the spectroscopic and X-ray crystallographic data presented herein along with previously reported mechanistic data for AAP, a new catalytic mechanism for the hydrolysis reaction catalyzed by AAP is proposed.
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{{ABSTRACT_PUBMED_11401547}}
==About this Structure==
==About this Structure==
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[[Category: Peptidase]]
[[Category: Peptidase]]
[[Category: Zinc]]
[[Category: Zinc]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 03:54:46 2008''

Revision as of 00:54, 1 July 2008

Image:1ft7.png

Template:STRUCTURE 1ft7

AAP COMPLEXED WITH L-LEUCINEPHOSPHONIC ACID

Template:ABSTRACT PUBMED 11401547

About this Structure

1FT7 is a Single protein structure of sequence from Vibrio proteolyticus. Full crystallographic information is available from OCA.

Reference

Inhibition of the aminopeptidase from Aeromonas proteolytica by L-leucinephosphonic acid. Spectroscopic and crystallographic characterization of the transition state of peptide hydrolysis., Stamper C, Bennett B, Edwards T, Holz RC, Ringe D, Petsko G, Biochemistry. 2001 Jun 19;40(24):7035-46. PMID:11401547

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