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Literature summary for 1.12.1.2 extracted from

  • Schmitz, O.; Boison, G.; Salzmann, H.; Bothe, H.; Schutz, K.; Wang, S.H.; Happe, T.
    HoxE - a subunit specific for the pentameric bidirectional hydrogenase complex (HoxEFUYH) of cyanobacteria (2002), Biochim. Biophys. Acta, 1554, 66-74.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
overexpression of HoxE in Escherichia coli strain M15 Synechocystis sp.

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.089
-
reduced methyl viologen pH 6.3, 60°C Synechocystis sp.

Metals/Ions

Metals/Ions Comment Organism Structure
additional information metalloenzyme Synechocystis sp.

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
18000
-
x * 18000, HoxE, SDS-PAGE, x * 21000, recombinant HIs-tagged HoxE, SDS-PAGE Synechocystis sp.
21000
-
x * 18000, HoxE, SDS-PAGE, x * 21000, recombinant HIs-tagged HoxE, SDS-PAGE Synechocystis sp.
375000
-
native dimeric assembly of the pentameric enzyme complex, gel filtration Synechocystis sp.

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
H2 + NAD+ Synechocystis sp.
-
H+ + NADH
-
r

Organism

Organism UniProt Comment Textmining
Synechocystis sp. Q9Z354 HoxE subunit from strain PCC 6301; strain PCC 6803, and strain PCC 6301 which is identical with Anacystis nidulans SAUG 1402-1
-

Oxidation Stability

Oxidation Stability Organism
enzyme is oxygen-labile Synechocystis sp.

Purification (Commentary)

Purification (Comment) Organism
under anaerobic conditions, pentameric bidirectional hydrogenase complex HoxEFUYH to near homogeneity 647fold from strain PCC 6803 and 1290fold from strain PCC 6301, recombinant His-tagged HoxE from Escherichia coli Synechocystis sp.

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
15
-
native purified enzyme complex from strain PCC 6301, hydrogen-forming activity, cofactor reduced methyl viologen Synechocystis sp.
67
-
native purified enzyme complex from strain PCC 6803, hydrogen-forming activity, cofactor reduced methyl viologen Synechocystis sp.

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
H2 + NAD(P)+
-
Synechocystis sp. H+ + NAD(P)H
-
r
H2 + NAD+
-
Synechocystis sp. H+ + NADH
-
r
H2 + oxidized dithionite
-
Synechocystis sp. H+ + reduced dithionite
-
r
H2 + oxidized methyl viologen
-
Synechocystis sp. H+ + reduced methyl viologen best cofactor r

Subunits

Subunits Comment Organism
? x * 18000, HoxE, SDS-PAGE, x * 21000, recombinant HIs-tagged HoxE, SDS-PAGE Synechocystis sp.
More the subunit HoxE, which is essential for the bidirectional hydrogenase activity, is included in a pentameric bidirectional hydrogenase complex HoxEFUYH in cyanobacteria, the complex forms dimer (HoxEFUYH)2, complex components are HoxE, HoxF, HoxH, HoxU, and HoxY, complex composition analysis, overview Synechocystis sp.

Synonyms

Synonyms Comment Organism
HoxE
-
Synechocystis sp.

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
60
-
strain PCC 6803, hydrogen-forming activity Synechocystis sp.

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
75
-
inactivation above Synechocystis sp.

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
6.3
-
strain PCC 6803, hydrogen-forming activity Synechocystis sp.

Cofactor

Cofactor Comment Organism Structure
additional information methyl viologen or dithionite can act as electron donor/acceptor Synechocystis sp.
additional information no activity with ferredoxin or FMN Synechocystis sp.
NAD(P)+
-
Synechocystis sp.
NAD(P)H NADH is 2times more active than NADPH Synechocystis sp.