Literature summary for 4.2.1.3 extracted from

Wuebbeler, J.H.; Bruland, N.; Kretschmer, K.; Steinbuechel, A.
Novel pathway for catabolism of the organic sulfur compound 3,3-dithiodipropionic acid via 3-mercaptopropionic acid and 3-Sulfinopropionic acid to propionyl-coenzyme A by the aerobic bacterium Tetrathiobacter mimigardefordensis strain DPN7 (2008), Appl. Environ. Microbiol., 74, 4028-4035.

Search for more literature for 4.2.1.3

Protein Variants

Protein Variants	Comment	Organism
additional information	transposon mutagenesis. In one disulfide 3,3-dithiodipropionic acid (DTDP)-negative (Jhw13b) and one DTDP-leaky (JhwAA14) mutant, Tn5::mob is mapped in a gene encoding a putative bifunctional aconitate hydratase 2/2-methylisocitrate dehydratase (AcnB, EC 4.2.1.3). AcnB dehydrates 2-methylcitric acid to 2-methyl-cis-aconitic acid and subsequently hydrates it to 2-methylisocitric acid	Advenella mimigardefordensis

Organism

Organism	UniProt	Comment	Textmining
Advenella mimigardefordensis	B3TZE0	-	-
Advenella mimigardefordensis DPN7T	B3TZE0	-	-

Synonyms

Synonyms	Comment	Organism
Aconitate hydratase	bifunctional enzyme: aconitate hydratase 2/2-methylisocitrate dehydratase	Advenella mimigardefordensis

Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.

Release 2023.1 (January 2023)