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Literature summary for 3.4.21.107 extracted from

  • Huesgen, P.F.; Miranda, H.; Lam, X.; Perthold, M.; Schuhmann, H.; Adamska, I.; Funk, C.
    Recombinant Deg/HtrA proteases from Synechocystis sp. PCC 6803 differ in substrate specificity, biochemical characteristics and mechanism (2011), Biochem. J., 435, 733-742.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 3.4.21.107

Cloned(Commentary)

Cloned (Comment) Organism
expressed in Escherichia coli BL21 Star (DE3) cells Synechocystis sp.

Protein Variants

Protein Variants Comment Organism
additional information deletion of the PDZ domain severely impairs proteolytic activity Synechocystis sp.
S237A inactive mutant of HhoA Synechocystis sp.
S258A inactive mutant of HhoB Synechocystis sp.
S296A inactive mutant of HtrA Synechocystis sp.

Metals/Ions

Metals/Ions Comment Organism Structure
Ca2+ the activity of recombinant HtrA and HhoA increases almost 4-6fold in the presence of 5 mM CaCl2 and remains constant at higher concentrations. The activity of recombinant HhoB increases more gradually up to 14fold, reaching the maximal level at 10 mM CaCl2. Almost no proteolytic activity is detected for recombinant HhoB in the absence of Ca2+ Synechocystis sp.
Mg2+ the activity of recombinant HtrA and HhoA increases almost 4-6fold in the presence of 5 mM MgCl2 and remains constant at higher concentrations. The activity of recombinant HhoB increases more gradually up to 14fold, reaching the maximal level at 10 mM MgCl2 Synechocystis sp.

Organism

Organism UniProt Comment Textmining
Synechocystis sp.
-
-
-

Purification (Commentary)

Purification (Comment) Organism
Ni-NTA column chromatography and His GraviTrap affinity column chromatography Synechocystis sp.

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
beta-casein + H2O little uncleaved beta-casein remains in assays with recombinant HtrA, and a prominent degradation fragment appears. Recombinant HhoA completely degrades the excess of beta-casein, whereas recombinant HhoB shows only little activity and generates a prominent degradation fragment with a slightly lower molecular mass than intact beta-casein. The C-terminal cleavage sites Val162, Gln141 and Val130 are identified for recombinant HtrA. A common cleavage site at Leu165 is found for HhoA and HhoB, however, HhoA additionally cleaves beta-casein at Ala101 generating two proteolytic fragments, the N-terminal 1-101 as well as the C-terminal 102-199 amino acid fragments Synechocystis sp. ?
-
 ?
BODIPY TR-X casein + H2O
-
 Synechocystis sp. ?
-
 ?
additional information no activity with correctly folded globular bovine serum albumin or lysozyme Synechocystis sp. ?
-
 ?

Subunits

Subunits Comment Organism
homotrimer
-
 Synechocystis sp.

Synonyms

Synonyms Comment Organism
DegP/HtrA
-
 Synechocystis sp.
HhoA HtrA homologue A Synechocystis sp.
HhoB HtrA homologue B Synechocystis sp.
high temperature requirement A protease
-
 Synechocystis sp.
HtrA
-
 Synechocystis sp.

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
35
-
 HhoB Synechocystis sp.
45
-
 HhoA Synechocystis sp.
50
-
 HtrA Synechocystis sp.

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
10 25 low proteolytic activity is recorded for the Deg/HtrA proteases HtrA, HhoA, and HhoB at a temperature ranging from 10 to 25°C Synechocystis sp.

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
5.5 6 HtrA in the absence of Ca2+ Synechocystis sp.
5.5 6.5 HhoB activity shows an optimum at pH 5.5-6.5 in the presence of 10 mM Ca2+ Synechocystis sp.
6.5
-
 HhoA in the absence of Ca2+ Synechocystis sp.
7
-
 HtrA in the presence of 10 mM Ca2+ Synechocystis sp.
8
-
 HhoA activity shows an optimum at pH 8.0 or higher in the presence of 10 mM Ca2+ Synechocystis sp.

General Information

General Information Comment Organism
physiological function HtrA, HhoA and HhoB are important for survival of Synechocystis sp. strain PCC 6803 under high light and temperature stresses. The three proteases may act as protein-quality-control factors degrading denatured and damaged proteins Synechocystis sp.