Any feedback?
Please rate this page
(all_enzymes.php)
(0/150)

BRENDA support

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

Engineering

Engineering on EC 3.4.21.97 - assemblin

Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
H61A
Herpes simplex virus
-
mutation impairs protease activity. Morphology of mutant capsids exclusively resembles those of procapsids or large cored B capsids. Specifically, mutant capsids are spherical and lack electron dense cores. Most of these particles are tightly clustered in the nucleoplasm. Mutant does not replicate to appreciable extents on CV1 cells
A133V
-
I-site mutant
A134Q
-
oligomerization at high protein concentration
A143Q
-
all enzyme samples used in this experiments contain an additional mutation, A143Q. The mutation disables one of the internal cleavage sites but has little effects on the kinetic properties of the enzyme
A143Q/D217N
-
the ratio of turnover number to Km-value is 11% of that for mutant enzyme A143Q
A143Q/D227N
-
the ratio of turnover number to Km-value is 1273fold lower than that for mutant A143Q
A143Q/E31R
-
the ratio of turnover number to Km-value is 44.6fold lower than that for the wild-typelike mutant A143Q
A143Q/E31S
-
the ratio of turnover number to Km-value is 4.8fold lower than that for the wild-typelike mutant A143Q
A143Q/H157A
-
the ratio of turnover number to Km-value is 22fold lower than that of the wild-typelike mutant enzyme A143Q
A143Q/H157E
-
the ratio of turnover number to Km-value is 11.7fold lower than that of the wild-typelike mutant enzyme A143Q
A143Q/H157Q
-
the ratio of turnover number to Km-value is 19fold lower than that of the wild-typelike mutant enzyme A143Q
A143Q/L229R
A143Q/R137E
-
the ratio of turnover number to Km-value is 6.3fold lower than that for the wild-typelike mutant A143Q
A143Q/R232H
-
mutant enzyme A143Q/R232H essentially maintains wild-type catalytic activity, shows little change in the CD spectra compared to mutant A143Q enzyme, thermal stability is similar to that of mutant A143Q enzyme. The ratio of turnover number to Km-value is 5.1fold lower than that for mutant enzyme A143Q
A143Q/S225Y
-
mutant enzyme with large conformational changes with 40% lower helical content relative to the mutant enzyme A143Q, mutant dimer has similar stability to the mutant A143Q dimer. Many of the conformational differences between the mutant A143Q and the mutant enzyme A143Q/S225Y are likely the direct result of the mutation itself. alphaF helix tilts away from the wild type dimer two-fold axis in the S225Y mutant, creating a space near the two-fold axis to accomodate the new Tyr side chain. The S225Y mutation is the likely trigger for the change in the monomer conformation and the dimer organization, significant lower thermal stability than the mutant enzyme A143Q. The ratio of turnover number to Km-value is 1273fold lower than that for mutant enzyme A143Q
A143Q/S225Y/L229R
-
mutation has little effect on the stability of the dimer, mutant enzyme with large conformational changes with 40% lower helical content relative to the mutant enzyme A143Q, significant lower thermal stability than the mutant enzyme A143Q. The ratio of turnover number to Km-value is 1680fold lower than that for mutant enzyme A143Q
A143T/A144T
-
mutant displays better stability than wild-type and has esterase activity toward specific small ester compounds, e.g., Boc-L-Ala-4-nitrophenol
A143V
-
inability of the mutant virus to effect I-site cleavage in infected cells, mutation has no gross effect on the rate of virus production or on the amounts of extracellular virions, noninfectious enveloped particles and dense bodies
H47A
-
inactive mutant, active if coexpressed with AW5 which encodes the first 179 amino acids of assemblin with the addition of Ile, Gln, Thr
S118A
-
inactive mutant, active if coexpressed with AW5 which encodes the first 179 amino acids of assemblin with the addition of Ile, Gln, Thr
S132A
S134A/A143Q
-
the ratio of turnover number to Km-value is 150fold lower than that of the wild-typelike mutant enzyme A143Q
S134A/A143Q/H157A
-
the ratio of turnover number to Km-value is 174fold lower than that of the wild-typelike mutant enzyme A143Q
V141G/V207G
-
soluble and stable, indistinguishable from wild-type in vitro
H47A
-
mutation prevents I-site cleavage (cleavage at an internal site of assemblin, converting it to a two-chain form that remain active). Imidazole restores I-site cleavage to mutant
additional information