Literature summary for 4.1.3.25 extracted from

Dimroth, P.; Buckel, W.; Loyal, R.; Eggerer, H.
Isolation and function of the subunits of citramalate lyase and formation of hybrids with the subunits of citrate lyase (1977), Eur. J. Biochem., 80, 469-477.

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Metals/Ions

Metals/Ions	Comment	Organism	Structure
Mg2+	required	Clostridium tetanomorphum
Mg2+	the isolated beta-subunit of citramalate lyase becomes saturated at 10 mM Mg2+	Clostridium tetanomorphum

Organism

Organism	UniProt	Comment	Textmining
Clostridium tetanomorphum	-	EC 4.1.3.25 is the beta-subunit of EC 4.1.3.22	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
(3S)-citramalyl-thio-acylcarrier protein	-	Clostridium tetanomorphum	?	-	?

Subunits

Subunits	Comment	Organism
More	EC 4.1.3.25 is the beta-subunit of EC 4.1.3.22	Clostridium tetanomorphum

Synonyms

Synonyms	Comment	Organism
More	EC 4.1.3.25 is the beta-subunit of EC 4.1.3.22	Clostridium tetanomorphum

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Release 2023.1 (January 2023)