Literature summary for 3.5.4.2 extracted from

Boitz, J.M.; Strasser, R.; Hartman, C.U.; Jardim, A.; Ullman, B.
Adenine aminohydrolase from Leishmania donovani: unique enzyme in parasite purine metabolism (2012), J. Biol. Chem., 287, 7626-7639.

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Inhibitors

Inhibitors	Comment	Organism	Structure
2'-deoxycoformycin	-	Leishmania donovani

KM Value [mM]

KM Value [mM]	KM Value Maximum [mM]	Substrate	Comment	Organism	Structure
0.0154	-	adenine	pH 7.0, 25°C	Leishmania donovani

Localization

Localization	Comment	Organism	GeneOntology No.	Textmining
cytosol	-	Leishmania donovani	5829	-

Molecular Weight [Da]

Molecular Weight [Da]	Molecular Weight Maximum [Da]	Comment	Organism
40800	-	SDS-PAGE	Leishmania donovani

Organism

Organism	UniProt	Comment	Textmining
Leishmania donovani	-	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
adenine + H2O	-	Leishmania donovani	hypoxanthine + NH3	-	?

Synonyms

Synonyms	Comment	Organism
AAH	-	Leishmania donovani

Turnover Number [1/s]

Turnover Number Minimum [1/s]	Turnover Number Maximum [1/s]	Substrate	Comment	Organism	Structure
16.75	-	adenine	pH 7.0, 25°C	Leishmania donovani

Ki Value [mM]

Ki Value [mM]	Ki Value maximum [mM]	Inhibitor	Comment	Organism	Structure
0.0231	-	2'-deoxycoformycin	pH 7.0, 25°C	Leishmania donovani

Expression

Organism	Comment	Expression
Leishmania donovani	Western blot analysis establishes that AAH is expressed in both life cycle stages of Leishmania donovani	additional information

General Information

General Information	Comment	Organism
malfunction	deletion of the AAH locus in intact parasites establishes that AAH is not an essential gene and that -/-aah cells are capable of salvaging the same range of purine nucleobases and nucleosides as wild type Leishmania donovani. The aah null mutant is able to infect murine macrophages in vitro and in mice, although the parasite loads in both model systems are modestly reduced compared with wild type infections	Leishmania donovani

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Release 2023.1 (January 2023)