GGH
GGH (gamma-glutamyl hydrolase, also known as GATD10) is a peptidase C26 family enzyme that removes gamma-linked glutamate residues from pteroylpolyglutamates. It acts on both folylpoly-gamma-glutamates and antifolylpoly-gamma-glutamates. Browse Assay Genie's current range of GGH research reagents below, or read on for the biology behind the target.
GGH hydrolyses the polyglutamate sidechains of pteroylpolyglutamates. It progressively removes gamma-glutamyl residues from pteroylpoly-gamma-glutamate, yielding pteroyl-alpha-glutamate (folic acid) and free glutamate. The NCBI Gene summary describes the same activity: the gene catalyses the hydrolysis of folylpoly-gamma-glutamates and antifolylpoly-gamma-glutamates by removing gamma-linked polyglutamates and glutamate.
Because of this activity, GGH is thought to play an important role in the bioavailability of dietary pteroylpolyglutamates. It is also thought to contribute to the metabolism of pteroylpolyglutamates and of antifolates, which makes it a relevant enzyme for researchers studying folate handling and antifolate biology. The enzyme is annotated as secreted into the extracellular space and as present in the lysosome and the melanosome.
The human GGH gene encodes a protein that belongs to the peptidase C26 family and is classified by HGNC within the glutamine amidotransferase class 1 domain containing group. The alias GATD10 reflects that grouping. Mouse and rat both carry a Ggh ortholog, so the enzyme can be studied in common rodent models. Assay Genie target pages for GGH bring together reagents for work on this folate-processing hydrolase, including studies of the GGH protein in different cellular compartments.
GGH removes gamma-glutamyl residues from pteroylpoly-gamma-glutamate to give folic acid and free glutamate, placing it within folate processing.
The enzyme hydrolyses antifolylpoly-gamma-glutamates and is implicated in antifolate metabolism, so it is relevant to studies of antifolate handling.
GGH may influence the bioavailability of dietary pteroylpolyglutamates, making it a point of interest in folate uptake and nutrition studies.
GGH is found in the extracellular space, lysosome and melanosome, offering a model for studying how one hydrolase acts across compartments.
GGH hydrolyses the polyglutamate sidechains of pteroylpolyglutamates. It progressively removes gamma-glutamyl residues to yield pteroyl-alpha-glutamate (folic acid) and free glutamate. It is also thought to contribute to the bioavailability of dietary pteroylpolyglutamates and to the metabolism of antifolates.
GGH stands for gamma-glutamyl hydrolase, and GATD10 is a listed alias. The enzyme carries the EC number 3.4.19.9. HGNC places it in the glutamine amidotransferase class 1 domain containing gene group, and UniProt assigns it to the peptidase C26 family.
Yes. Mouse and rat each have an ortholog named Ggh, which allows the enzyme to be studied in rodent models. Cross-species work should always be checked against the datasheet of any product for its validated reactivity.
Other folate-pathway enzymes and transporters that sit alongside GGH in folate and antifolate research.
Gene and protein annotations from HGNC, NCBI Gene and UniProt Q92820; product specifications from Assay Genie datasheets.