Recombinant Human GALNT10 Protein Standard (His tag)

Supplementary info

This supplementary information is collated from multiple sources and compiled automatically.

Activity summary

GALNT10 also known as polypeptide N-acetylgalactosaminyltransferase 10 is a member of the GalNAc-T family of enzymes. The enzyme plays an important mechanical role by catalyzing the transfer of N-acetylgalactosamine (GalNAc) to serine and threonine residues on proteins a process called O-glycosylation. This enzymatic activity is critical for proper protein modification and function. GALNT10 has a molecular mass of approximately 68 kDa. It is expressed in a variety of tissues notably in the liver which indicates its extensive role in protein processing within this organ.

Biological function summary

Polypeptide N-acetylgalactosaminyltransferase 10 influences the initial steps of mucin-type O-glycosylation which significantly affects protein stability and cell signaling. It is not part of a large enzyme complex but its function is integral to the regulation of substrate-specific modifications. This protein aids in the modulation of various glycoproteins impacting diverse physiological processes. Alterations in its activity potentially lead to changes in cell-cell interactions and mucosal protection.

Pathways

GALNT10 is involved in O-glycan biosynthetic pathways where its role is pivotal in glycan structure formation and diversity. This pathway enables the proper glycosylation of proteins that are essential for cell-cell communication and adhesion. GALNT10's activity relates closely to other glycosyltransferases within this pathway including GALNT1 reflecting its cooperative nature within glycosylation networks. Moreover it supports the broader glycosylation landscape by influencing the availability of glycosylation sites on various protein substrates.

Associated diseases and disorders

GALNT10 has associations with specific conditions such as cancers and metabolic syndromes. Abnormal function or expression of this enzyme can contribute to tumorigenesis due to its influence on glycosylation patterns that affect cell adhesion and signaling. The enzyme is also linked to liver disorders arising from its high expression in liver tissue and its impact on protein processing. In the context of cancer GALNT10’s interactions with similar glycosylation enzymes like GALNT3 illustrate its role in modifying glycan structures which are critical for cellular transformation and cancer progression.