Literature summary for 2.5.1.17 extracted from

Padovani, D.; Banerjee, R.
A rotary mechanism for coenzyme B(12) synthesis by adenosyltransferase (2009), Biochemistry, 48, 5350-5357.

Search for more literature for 2.5.1.17

Cloned(Commentary)

Cloned (Comment)	Organism
recombinantly expressed in Escherichia coli	Methylorubrum extorquens

Organism

Organism	UniProt	Comment	Textmining
Methylorubrum extorquens	-	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
ATP + cob(I)alamin	binding of the substrate ATP to ATR that is fully loaded with 5'-deoxyadenosylcobalamin leads to the ejection of 1 equivalent of the cofactor into solution. In the presence of methylmalonyl-CoA mutase and ATP, 5'-deoxyadenosylcobalamin is transferred from ATR to the acceptor protein in a process that exhibits an 3.5fold lower Kact for ATP compared to the one in which cofactor is released into solution. ATP favorably influences cofactor transfer in the forward direction by reducing the ratio of apo-methylmalonyl-CoA mutase/holo-ATR required for delivery of 1 equivalent of 5'-deoxyadenosylcobalamin, from 4 to 1. A rotary rotary mechanism for ATR function is proposed in which, at any given time, only two of its active sites are used for 5'-deoxyadenosylcobalamin synthesis and where binding of ATP to the vacant site leads to the transfer of the high value 5'-deoxyadenosylcobalamin product to the acceptor mutase	Methylorubrum extorquens	triphosphate + adenosylcob(III)alamin	-	?

Synonyms

Synonyms	Comment	Organism
ATR	-	Methylorubrum extorquens

Temperature Optimum [°C]

Temperature Optimum [°C]	Temperature Optimum Maximum [°C]	Comment	Organism
20	-	assay at	Methylorubrum extorquens

pH Optimum

pH Optimum Minimum	pH Optimum Maximum	Comment	Organism
8	-	assay at	Methylorubrum extorquens

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Release 2023.1 (January 2023)