Literature summary for 5.4.3.5 extracted from

Tseng, C.H.; Yang, C.H.; Lin, H.J.; Wu, C.; Chen, H.P.
The S subunit of D-ornithine aminomutase from Clostridium sticklandii is responsible for the allosteric regulation in D-alpha-lysine aminomutase (2007), FEMS Microbiol. Lett., 274, 148-153.

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Cloned(Commentary)

Cloned (Comment)	Organism
enzyme S subunit OraS, expression in Escherichia coli	Acetoanaerobium sticklandii

Protein Variants

Protein Variants	Comment	Organism
additional information	protein KamDE comprised of the 30000 and 51000 Da subunits of the E1 component of D-alpha-lysine aminomutase is catalytically active in absence of the third 12800 kDa subunit, but ATP no longer has a regulatory effect on it. The S subunit of D-ornithine aminomutase, OraS, is capable of forming a complex with KamDE and restores the enzymes ATP-dependent allosteric regulation. OraS protein alone lowers the Km of KamDE for adenosylcobalamin and pyridoxal phosphate	Acetoanaerobium sticklandii

Organism

Organism	UniProt	Comment	Textmining
Acetoanaerobium sticklandii	-	-	-

Purification (Commentary)

Purification (Comment)	Organism
enzyme S subunit OraS, expression in Escherichia coli	Acetoanaerobium sticklandii

Subunits

Subunits	Comment	Organism
More	protein KamDE comprised of the 30000 and 51000 Da subunits of the E1 component of D-alpha-lysine aminomutase is catalytically active in absence of the third 12800 kDa subunit, but ATP no longer has a regulatory effect on it. The S subunit of D-ornithine aminomutase, OraS, is capable of forming a complex with KamDE and restores the enzymes ATP-dependent allosteric regulation	Acetoanaerobium sticklandii

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Release 2023.1 (January 2023)