Literature summary for 1.14.14.18 extracted from

Davydov, R.; Fleischhacker, A.S.; Bagai, I.; Hoffman, B.M.; Ragsdale, S.W.
Comparison of the mechanisms of heme hydroxylation by heme oxygenases-1 and -2 Kinetic and cryoreduction studies (2016), Biochemistry, 55, 62-68 .

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Cloned(Commentary)

Cloned (Comment)	Organism
-	Homo sapiens

Protein Variants

Protein Variants	Comment	Organism
additional information	a variant of Hmox1 lacking the C-terminal heme regulatory domain exhibits the same specific activity as one containing both the catalytic core and heme regulatory domain. A truncated variant containing only the heme regulatory region binds but cannot oxidize heme	Homo sapiens

Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	P30519	isoform Hmox2	-

Synonyms

Synonyms	Comment	Organism
heme oxygenase 2	-	Homo sapiens
Hmox2	-	Homo sapiens

General Information

General Information	Comment	Organism
physiological function	isoform Hmox2 contains two C-terminal heme regulatory motifs centered at Cys265 and Cys282. The same mechanism of heme hydroxylation to alpha-meso-hydroxyheme is employed by both isoform Hmox1 and Hmox2 and the heme regulatory motifs do not affect the physicochemical properties of the oxy-Fe(II) and HOO-Fe(III) states of Hmox2. Heme oxygenation by Hmox2 occurs solely at the catalytic core and hydroxylation proceeds three times slower and the oxy-Fe(II) state is 100fold less stable in Hmox2 than in Hmox1	Homo sapiens

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Release 2023.1 (January 2023)