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3.4.23.B4: Feline immunodeficiency virus protease

This is an abbreviated version!
For detailed information about Feline immunodeficiency virus protease, go to the full flat file.

Word Map on EC 3.4.23.B4

Reaction

the enzyme seems to have a preference for Val in P1' and Phe in P1. In contrast to the HIV-1 protease the feline immunodeficiency virus protease does not cleave the peptide KSGVFVQNGLVK at the Phe-Val bond. Gln in P2' may be inhibitory. In contrast to HIV-1 protease the feline immunodeficiency virus protease does not cleave peptide KSGNFVVNGLVK at the Phe-Val bond. Asn in P2 may be inhibitory =

Synonyms

FCV protease, feline immunodeficiency virus protease, Feline immunodeficiency virus retropepsin, FIV PR, FIV protease, FIV retropepsin, FIV-PR, More

ECTree

     3 Hydrolases
         3.4 Acting on peptide bonds (peptidases)
             3.4.23 Aspartic endopeptidases
                3.4.23.B4 Feline immunodeficiency virus protease

Crystallization

Crystallization on EC 3.4.23.B4 - Feline immunodeficiency virus protease

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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
complex of the D30N mutant enzyme with the statine-based inhibitor LP-149 as well as with a substrate based on a modification of the inhibitor, LP-149S
crystal structure (1.7 A) of FIV protease is obtained in which 12 critical residues around the active site have been substituted with the structurally equivalent residues of HIV PR (12XFIV PR). The chimeric PR is crystallized in complex with inhibitor TL-3. Comparison of the crystal structures of the TL-3 complexes of 12X FIV and wild-type FIV PR reveal the information of additional van der Waals interactions between the enzyme inhibitor in the mutant PR
crystal structure determination and analysis, recombinant enzyme
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hanging-drop vapor diffusion technique, crystals are grown at 4°C, crystal structure of the enzyme in complex with LP-130
mutant I37V/N55M/V59I/I98S/Q99V/P100N in complex with HIV inhibitors darunavir and lopinavir, to 1.7 and 1.8 A resolution, respectively. A flexible 90s loop and residue 98 play roles in supporting Gag processing and infectivity, residue 37 is involved in the active site and residues 55, 57 and 59 in the flap in conferring the ability to specifically recognize HIV PR drugs. Ile37Val preserves tertiary structure but prevents steric clashes with the inhibitors. Asn55Met and Val59Ile induce a distinct kink in the flap and a new hydrogen bond to darunavir. Ile98Pro-Ser and Pro100Asn increase 90s loop flexibility, Gln99Val contributes hydrophobic contacts to the inhibitors, and Pro100Asn forms compensatory hydrogen bonds
structure of enzyme-inhibitor complex with LP-149
the two enzymes FIV protease and HIV-1 protease are strikingly similar at the crystallographic level, particularly within the substrate binding region
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wild-type and mutant enzymes V59I and Q99V are cocrystallized with the C2-symmetric inhibitor TL-3, which contains (1S,2R,3R,4S)-1,4-diamino-1,4-dibenzyl-2,3-diol as the P1-P1' unit and Ala at P3/P3' positions
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