Literature summary for 1.14.14.18 extracted from

Soldano, A.; Klinke, S.; Otero, L.H.; Rivera, M.; Catalano-Dupuy, D.L.; Ceccarelli, E.A.
Structural and mutational analyses of the Leptospira interrogans virulence-related heme oxygenase provide insights into its catalytic mechanism (2017), PLoS ONE, 12, e0182535 .

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Cloned(Commentary)

Cloned (Comment)	Organism
expression in Escherichia coli	Leptospira interrogans serovar Icterohaemorrhagiae

Crystallization (Commentary)

Crystallization (Comment)	Organism
heme oxygenase-heme complex at 1.73 A resolution. A hydrogen-bonded network of structural water molecules that extends from the catalytic site to the protein surface is observed. A long-range communication exists between the outer fringes of the hydrogen-bonded network of structural waters and the heme active site during catalysis. Model for the productive association of ferredoxin-NADP+ reductase and heme oxygenase	Leptospira interrogans serovar Icterohaemorrhagiae

Crystallization (Comment)

Organism

heme oxygenase-heme complex at 1.73 A resolution. A hydrogen-bonded network of structural water molecules that extends from the catalytic site to the protein surface is observed. A long-range communication exists between the outer fringes of the hydrogen-bonded network of structural waters and the heme active site during catalysis. Model for the productive association of ferredoxin-NADP+ reductase and heme oxygenase

Leptospira interrogans serovar Icterohaemorrhagiae

Protein Variants

Protein Variants	Comment	Organism
F157A	mutant is unable to carry out the complete degradation of heme to biliverdin, the reaction is arrested at the verdoheme stage. The protein displays bands at 357, 525 and 678 nm, reminiscent of the absorption spectrum reported for the HO-verdoheme complex. Overexpression of the HO F157 variants causes the Escherichia coli cells to turn dark green color	Leptospira interrogans serovar Icterohaemorrhagiae
F157I	mutant is unable to carry out the complete degradation of heme to biliverdin, the reaction is arrested at the verdoheme stage. The protein displays bands at 357, 525 and 678 nm, reminiscent of the absorption spectrum reported for the HO-verdoheme complex. Overexpression of the HO F157 variants causes the Escherichia coli cells to turn dark green color	Leptospira interrogans serovar Icterohaemorrhagiae
additional information	a C26S variant lacking the last 20 C-terminal residues incorporates the prosthetic group efficiently and is active	Leptospira interrogans serovar Icterohaemorrhagiae

KM Value [mM]

KM Value [mM]	KM Value Maximum [mM]	Substrate	Comment	Organism	Structure
0.00177	-	[reduced NADPH-hemoprotein reductase]	wild-type, pH 7.5, 25°C	Leptospira interrogans serovar Icterohaemorrhagiae
0.00271	-	[reduced NADPH-hemoprotein reductase]	mutant F157I, pH 7.5, 25°C	Leptospira interrogans serovar Icterohaemorrhagiae

Organism

Organism	UniProt	Comment	Textmining
Leptospira interrogans serovar Icterohaemorrhagiae	-	-	-
Leptospira interrogans serovar Icterohaemorrhagiae serovar Lai 56601	-	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
heme + [reduced NADPH-hemoprotein reductase] + O2	-	Leptospira interrogans serovar Icterohaemorrhagiae	biliverdin + Fe2+ + CO + [oxidized NADPH-hemoprotein reductase] + H2O	-	?
heme + [reduced NADPH-hemoprotein reductase] + O2	-	Leptospira interrogans serovar Icterohaemorrhagiae serovar Lai 56601	biliverdin + Fe2+ + CO + [oxidized NADPH-hemoprotein reductase] + H2O	-	?