Fumarate reductase

Enzyme converting fumarate to succinate From Wikipedia, the free encyclopedia

Fumarate reductase is the enzyme that converts fumarate to succinate, and is important in microbial metabolism as a part of anaerobic respiration.[1] The catalyzed reaction is:

succinate + acceptor ↔ fumarate + reduced acceptor

Fumarate reductases can be divided into three classes depending on the electron acceptor:

+ NADH
 
 
H+
 
Reversible left-right reaction arrow with minor forward substrate(s) from top left and minor reverse product(s) to bottom left
H+
 
 
+ NAD+
 
The enzyme is monomeric and soluble, and can reduce fumarate independently from the electron transport chain.[2] Fumarate reductase is absent from all mammalian cells.
  • Fumarate reductase (CoM/CoB) (EC 1.3.4.1):
    This enzyme is present in most methanogenic archea. It is cytoplasmic and uses coenzymes M and B as hydrogen donors.[3]
  • Fumarate reductase (quinol) (EC 1.3.5.1)
    The membrane-bound enzyme covalently linked to flavin cofactors, which is composed of 3 or 4 subunits, transfers electrons from a quinol to fumarate. This class of enzyme is thus involved in the production of ATP by oxidative phosphorylation.[1]

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