Literature summary for 4.1.1.111 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 .

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Cloned(Commentary)

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

Crystallization (Commentary)

Crystallization (Comment)	Organism
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
to 2.0 A resolution	Hydrogenobacter thermophilus

Protein Variants

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

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

Organism

Organism	UniProt	Comment	Textmining
Hydrogenobacter thermophilus	D3DFS4	-	-
Hydrogenobacter thermophilus DSM 6534	D3DFS4	-	-

Purification (Commentary)

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

Substrates and Products (Substrate)

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

Synonyms

Synonyms	Comment	Organism
nirDL	-	Hydrogenobacter thermophilus