Literature summary for 1.14.14.18 extracted from

Huber, W.J.; Marohnic, C.C.; Peters, M.; Alam, J.; Reed, J.R.; Masters, B.S.; Backes, W.L.
Measurement of membrane-bound human heme oxygenase-1 activity using a chemically defined assay system (2009), Drug Metab. Dispos., 37, 857-864.

Search for more literature for 1.14.14.18

Activating Compound

Activating Compound	Comment	Organism	Structure
additional information	a higher dilauroylphosphatidylcholine/HO-1 ratio than typically used provides an improved environment for HO-1 activity	Homo sapiens

Cloned(Commentary)

Cloned (Comment)	Organism
-	Homo sapiens

Protein Variants

Protein Variants	Comment	Organism
R254K	enhances protein stability during the glutathione S-transferase-tag removal procedure involving the protease thrombin	Homo sapiens

Inhibitors

Inhibitors	Comment	Organism	Structure
additional information	HO-1-generated hydrogen peroxide leads to a decrease in HO-1 activity	Homo sapiens

Localization

Localization	Comment	Organism	GeneOntology No.	Textmining
membrane	presence of the membrane-spanning region on HO-1 is required for efficient membrane incorporation, which is achieved after a 2 h preincubation period at room temperature	Homo sapiens	16020	-

Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	-	-	-

Purification (Commentary)

Purification (Comment)	Organism
-	Homo sapiens

Storage Stability

Storage Stability	Organism
-80°C	Homo sapiens

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
heme + electron donor + O2	-	Homo sapiens	biliverdin + Fe2+ + CO + oxidized electron donor + H2O	-	?
additional information	ability of uncoupled HO-1 to produce large quantities of H2O2, H2O2 generation is much more efficient with the full-length form of HO-1 than with the soluble form	Homo sapiens	?	-	?

Synonyms

Synonyms	Comment	Organism
heme oxygenase-1	-	Homo sapiens
HO-1	-	Homo sapiens

Cofactor

Cofactor	Comment	Organism	Structure
heme	-	Homo sapiens

General Information

General Information	Comment	Organism
physiological function	because HO-1 and NADPH-cytochrome P450 reductase (CPR) are membrane-bound proteins, the presence of membrane hydrophobic milieu (dilauroylphosphatidylcholine or endoplasmic reticulum membrane) may alter the mechanism by which cytosolic biliverdin reductase metabolizes its substrate biliverdin to bilirubin	Homo sapiens

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Release 2023.1 (January 2023)