Although hGMPR1 and hGMPR2 do not have an identical amino acid sequence, they have similar kinetic properties and they both use NADPH as a coenzyme for their catalyzed reaction.

[7] A crystal structure of hGMPR2 was obtained, and the model shows that hGMPR2 is a homotetramer that consist of a mix of alpha helices and beta sheets (parallel and antiparallel).

[8] Inosine monophosphate dehydrogenase (IMPDH) and GMPR have similar catalytic mechanisms but different structural dynamics.

[3] The rat version of GMPR is expressed in brown adipose tissue (BAT) when certain conditions triggers its response and it is mainly present in the kidney, as well as cardiac and skeletal muscle.

When the organism is exposed to the cold, the GMPR RNA expression can increase to a maximum of 30 fold, allowing heat production.

A hypothesis for this occurring is that the conversion of GMP to IMP potentially increase adenylosuccinate (precursor of AMP), which allows for the production of a second messenger cAMP.

The presence of the adenosine can bind to A1/A2 receptors (important for mediation of Tau phosphorylation) which ultimately results in increased expression of Alzheimer's disease.

Activation of the adenosine receptors increases the tangling of neurofilaments so Alzheimer's disease patients' conditions will worsen.

It has been found that in the cases of promyelocytic leukemia cells being differentiate to monocytes, the expression of GMPR has increased by a lot.