Guanidino acid hydrolase, mitochondrial (AGMAT)

Guanidino acid hydrolase, mitochondrial (formerly annotated as agmatinase, AGMAT) is a mitochondrial enzyme in the ureohydrolase family that was originally believed to catalyze the hydrolysis of agmatine to putrescine and urea[3]. However, recent studies conclusively show that human AGMAT is virtually inactive toward agmatine and instead efficiently hydrolyzes linear guanidino acids such as guanidinobutyrate and taurocyamine[2]. AGMAT possesses a structural fold and catalytic site similar to arginase family enzymes, including dependence on manganese ions for activity[1][2]. Its physiological function in humans is best described as the regulation of various guanidino acids, and not agmatine directly. While agmatine plays roles in neurotransmission and cellular signaling[1], AGMAT's function is related to broader guanidino acid metabolism. The gene is AGMAT in humans, but the enzyme is not established as a current therapeutic target and has limited direct disease links or established pharmacology[2][3]. Important note: The original annotation of AGMAT as "agmatinase" for the human enzyme is likely incorrect; recent evidence strongly indicates its canonical substrate is not agmatine but other guanidino acids[2]. Thus, sequence- or annotation-based references to "agmatinase" for human AGMAT should be considered obsolete or potentially misleading. The field is shifting to the use of the name "guanidino acid hydrolase, mitochondrial (AGMAT)" for human protein[2].

Other names

Guanidino acid hydrolase, mitochondrialAGMATGDAHFLJ23384Arginase, mitochondrialGuanidinobutyrase, mitochondrialGuanidinopropionase, mitochondrialguanidino acid hydrolase, mitochondrialagmatinase, mitochondrialagmatine ureohydrolase (agmatinase)

Catalyzes hydrolysis of guanidino acids to corresponding amine and urea. For agmatinase orthologs: hydrolyzes agmatine to putrescine and urea.