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

BRENDA support

Literature summary extracted from

  • Haufschildt, K.; Schmelz, S.; Kriegler, T.M.; Neumann, A.; Streif, J.; Arai, H.; Heinz, D.W.; Layer, G.
    The crystal structure of siroheme decarboxylase in complex with iron-uroporphyrin III reveals two essential histidine residues (2014), J. Mol. Biol., 426, 3272-3286 .
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
4.1.1.111 expressed in Escherichia coli BL21(DE3) cells Hydrogenobacter thermophilus

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
4.1.1.111 in complex with iron-uroporphyrin III, sitting drop vapor diffusion method, using 19% (w/v) polyethylene glycol 3350, 0.1 M sodium citrate (pH 5.6), 0.18 M LiCl and 6.7 mM 4-aminobenzoic acid Hydrogenobacter thermophilus
4.1.1.111 to 2.0 A resolution Hydrogenobacter thermophilus

Protein Variants

EC Number Protein Variants Comment Organism
4.1.1.111 H226Q activity similar to wild-type Hydrogenobacter thermophilus
4.1.1.111 H226Q the mutant shows impaired iron-uroporphyrin III binding while its overall activity is comparable to the wild type enzyme Hydrogenobacter thermophilus
4.1.1.111 H261A almost complete inactivation. No significant changes in the characteristic absorption spectrum of the substrate analogue Fe-URO III Hydrogenobacter thermophilus
4.1.1.111 H261A the mutation leads to the almost complete inactivation of the enzyme Hydrogenobacter thermophilus
4.1.1.111 H261S almost complete inactivation. No significant changes in the characteristic absorption spectrum of the substrate analogue Fe-URO III Hydrogenobacter thermophilus
4.1.1.111 H261S the mutation leads to the almost complete inactivation of the enzyme Hydrogenobacter thermophilus
4.1.1.111 H93A almost complete inactivation. Mutant shows similar spectral changes upon binding of substrate analogue Fe-URO III as wild-type Hydrogenobacter thermophilus
4.1.1.111 H93A the mutation leads to the almost complete inactivation of the enzyme Hydrogenobacter thermophilus
4.1.1.111 H93Q 93% decrease in activity Hydrogenobacter thermophilus
4.1.1.111 H93Q the mutation leads to the almost complete inactivation of the enzyme Hydrogenobacter thermophilus
4.1.1.111 H93S almost complete inactivation. Mutant shows similar spectral changes upon binding of substrate analogue Fe-URO III as wild-type Hydrogenobacter thermophilus
4.1.1.111 H93S the mutation leads to the almost complete inactivation of the enzyme Hydrogenobacter thermophilus
4.1.1.111 R218A activity similar to wild-type Hydrogenobacter thermophilus
4.1.1.111 R218A the mutant shows impaired iron-uroporphyrin III binding while its overall activity is comparable to the wild type enzyme Hydrogenobacter thermophilus
4.1.1.111 R218K activity similar to wild-type Hydrogenobacter thermophilus
4.1.1.111 R218K the mutant shows iron-uroporphyrin III binding and overall activity which are comparable to the wild type enzyme Hydrogenobacter thermophilus
4.1.1.111 R219Q the mutant shows impaired iron-uroporphyrin III binding while its overall activity is comparable to the wild type enzyme Hydrogenobacter thermophilus
4.1.1.111 R219Q, activity similar to wild-type Hydrogenobacter thermophilus
4.1.1.111 Y263F activity similar to wild-type Hydrogenobacter thermophilus
4.1.1.111 Y263F the mutant shows impaired iron-uroporphyrin III binding while its overall activity is comparable to the wild type enzyme Hydrogenobacter thermophilus
4.1.1.111 Y95L activity similar to wild-type Hydrogenobacter thermophilus
4.1.1.111 Y95L the mutant shows impaired iron-uroporphyrin III binding while its overall activity is comparable to the wild type enzyme Hydrogenobacter thermophilus

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
4.1.1.111 siroheme Hydrogenobacter thermophilus
-
 12,18-didecarboxysiroheme + CO2
-
 r
4.1.1.111 siroheme Hydrogenobacter thermophilus DSM 6534
-
 12,18-didecarboxysiroheme + CO2
-
 r

Organism

EC Number Organism UniProt Comment Textmining
4.1.1.111 Hydrogenobacter thermophilus D3DFS4
-
-
4.1.1.111 Hydrogenobacter thermophilus DSM 6534 D3DFS4
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
4.1.1.111 Ni-NTA column chromatography and Superdex 75 gel filtration Hydrogenobacter thermophilus

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4.1.1.111 12,18-didecarboxysiroheme + CO2 100% activity Hydrogenobacter thermophilus siroheme
-
 r
4.1.1.111 12,18-didecarboxysiroheme + CO2 100% activity Hydrogenobacter thermophilus DSM 6534 siroheme
-
 r
4.1.1.111 monodecarboxysiroheme 2.9% activity compared to 12,18-didecarboxysiroheme Hydrogenobacter thermophilus ?
-
 ?
4.1.1.111 monodecarboxysiroheme 2.9% activity compared to 12,18-didecarboxysiroheme Hydrogenobacter thermophilus DSM 6534 ?
-
 ?
4.1.1.111 siroheme
-
 Hydrogenobacter thermophilus 12,18-didecarboxysiroheme + 2 CO2
-
 ?
4.1.1.111 siroheme
-
 Hydrogenobacter thermophilus DSM 6534 12,18-didecarboxysiroheme + 2 CO2
-
 ?
4.1.1.111 siroheme
-
 Hydrogenobacter thermophilus 12,18-didecarboxysiroheme + CO2
-
 r
4.1.1.111 siroheme
-
 Hydrogenobacter thermophilus DSM 6534 12,18-didecarboxysiroheme + CO2
-
 r

Synonyms

EC Number Synonyms Comment Organism
4.1.1.111 nirDL
-
 Hydrogenobacter thermophilus