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3.4.21.97: assemblin

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

Word Map on EC 3.4.21.97

Reaction

Cleaves -Ala-/-Ser- and -Ala-/-Ala- bonds in the scaffold protein =

Synonyms

Assemblin, assembly protein precursor-processing proteinase, capsid scaffolding protein, cytomegalovirus protease, cytomegalovius maturational protease, cytomeglovirus protease, HCMV protease, Herpes simplex virus 1 proteinase Pra, Herpes simplex virus endopeptidase, HHV-6 proteinase, hMCV, HSV 1 protease, HSV-1, HSV-1 protease, HSV-2, human cytomegalovirus maturational protease, human cytomegalovirus maturational proteinase, human cytomegalovirus protease, human cytomegalovirus proteinase, maturation proteinase, proteinase, assembly protein precursor-processing, pUL80a, SFA, Varicella-zoster virus gene 33 proteinase

ECTree

     3 Hydrolases
         3.4 Acting on peptide bonds (peptidases)
             3.4.21 Serine endopeptidases
                3.4.21.97 assemblin

Crystallization

Crystallization on EC 3.4.21.97 - assemblin

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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystal structure of HAS-2 with covalently bound diisopropyl fluorophosphate
Herpes simplex virus
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in complex with inhibitors {N-[2-benzyl-4-(1H-tetrazol-5-yl)phenyl]-6-(cyclohexylmethyl)pyridine-2-carboxamide and N-[2-benzyl-4-[(methylsulfonyl)carbamoyl]phenyl]-6-(cyclohexylmethyl)pyridine-2-carboxamide
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crystal structure at 2.0 A resolution
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crystal structure at 2.27 A resolution
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crystal structure of HCMV protease in complex with the peptidomimetic inhibitor BILC 821 as protease model. Only the dimeric form of the protease is able to reorient the main-chain atoms of Arg165 along the reaction coordinate in order to stabilize more efficiently the oxyanion formed in the reaction pathway
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crystal structure of the catalytic domain at 2.5 A resolution
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hanging drop method, microseeding technique, each of six components in the final crystallization formula (16% polyethylene glycol 4000, 0.1 M MES pH 6.0, 0.4 M LiCl, 10% glycerol 5% tert-butanol and 5 mM Na2S2O3) plays a distinctive role and is indispensable. Free enzyme crystallizes at pH 6.0. Using 20-50 mM spermine in the crystallization buffer, crystals of two peptidomimetic inhibitor complexes with C821 are obtained at pH 7.5 and pH 8.0. Spermine is required for the inhibitor complexes to be crystallized at pH 8.0, possibly neutralizing net negative charges of the enzyme owing to its acidic pI of 5.5
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hanging drop vapour diffusion method, wild-type and mutant enzymes
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hanging-drop vapor diffusion method, crystal structure of the wild-typelike mutant enzyme A143Q in complex with peptidomimetic inhibitors, crystal structure of peptidomimetic inhibitor in complex with the E31R mutant enzyme
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in complex with inhibitors 3_4_21-97_3-cp2 and 3_4_21-97_3-cp3
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sitting-drop vapour diffusion method, crystals of the S225Y mutant in complex with the peptidomimetic inhibitor BILC408
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in complex with inhibitors 3_4_21-97_3-cp2 and 3_4_21-97_3-cp3
structures of native monomeric, active dimeric, and diisopropyl fluorophosphate-inhibited dimeric protease, to respective resolutions of 2.05, 2.10 and 2.03 A. In the dimeric form, a functional oxyanion hole is formed by a loop of 10 aminoacid residues encompassing two consecutive arginine residues (Arg136 and Arg137). In the monomeric form, the top of the loop is shifted by approximately 11 A, resulting in a complete disruption of the oxyanion hole and loss of activity. The dimerization-induced allosteric changes are basis for the concentration-dependent activation of the protease