This enzyme, along with protein farnesyltransferase (EC 2.5.1.58) and protein geranylgeranyltransferase type II (EC 2.5.1.60), constitutes the protein prenyltransferase family of enzymes. Catalyses the formation of a thioether linkage between the C-1 atom of the geranylgeranyl group and a cysteine residue fourth from the C-terminus of the protein. These protein acceptors have the C-terminal sequence CA1A2X, where the terminal residue, X, is preferably leucine; serine, methionine, alanine or glutamine makes the protein a substrate for EC 2.5.1.58. The enzymes are relaxed in specificity for A1, but cannot act if A2 is aromatic. Known targets of this enzyme include most gamma-subunits of heterotrimeric G proteins and Ras-related GTPases such as members of the Ras and Rac/Rho families. A zinc metalloenzyme. The Zn2+ is required for peptide, but not for isoprenoid, substrate binding.
ggtase-i, ggtase i, ggtase, geranylgeranyltransferase i, pggt-i, cdc43, protein geranylgeranyltransferase type i, geranylgeranyltransferase type i, protein geranylgeranyltransferase, protein geranylgeranyltransferase-i, more
This enzyme, along with protein farnesyltransferase (EC 2.5.1.58) and protein geranylgeranyltransferase type II (EC 2.5.1.60), constitutes the protein prenyltransferase family of enzymes. Catalyses the formation of a thioether linkage between the C-1 atom of the geranylgeranyl group and a cysteine residue fourth from the C-terminus of the protein. These protein acceptors have the C-terminal sequence CA1A2X, where the terminal residue, X, is preferably leucine; serine, methionine, alanine or glutamine makes the protein a substrate for EC 2.5.1.58. The enzymes are relaxed in specificity for A1, but cannot act if A2 is aromatic. Known targets of this enzyme include most gamma-subunits of heterotrimeric G proteins and Ras-related GTPases such as members of the Ras and Rac/Rho families. A zinc metalloenzyme. The Zn2+ is required for peptide, but not for isoprenoid, substrate binding.
high enzyme activity. GGTI expression and activity are particularly enriched in the adult brain and developmentally regulated after birth in various mammalian tissues
high enzyme activity. GGTI expression and activity are particularly enriched in the adult brain and developmentally regulated after birth in various mammalian tissues
mice with lateral ventricular injection of GGTi-2147, a specific GGTI inhibitor, have significant reduction in the membrane association of Rac1 and in the dendritic spine densities in the hippocampus, the cerebellum, and the frontal cortex
role of geranylgeranyltransferase I-mediated protein prenylation in the brain. GGTI and geranylgeranylation are involved in neurodegenerative diseases, e.g., aging, Alzheimer's disease, multiple sclerosis, and Niemann-Pick disease type C, mechanism of GGTI-mediated isoprenylation in the pathogenesis of neurodegenerative and neurodevelopmental disorders, overview. Importance of prenylation in synaptic function. GGTI not only regulates the basal neuronal dendritic growth but also mediates neuronal activity and BDNF-induced dendritogenesis. GGTI promotes neuronal dendritogenesis via increasing the membrane association of Rac1 in CNS neurons
mice with lateral ventricular injection of GGTi-2147, a specific GGTI inhibitor, have significant reduction in the membrane association of Rac1 and in the dendritic spine densities in the hippocampus, the cerebellum, and the frontal cortex
role of geranylgeranyltransferase I-mediated protein prenylation in the brain. GGTI and geranylgeranylation are involved in neurodegenerative diseases, e.g., aging, Alzheimer's disease, multiple sclerosis, and Niemann-Pick disease type C, mechanism of GGTI-mediated isoprenylation in the pathogenesis of neurodegenerative and neurodevelopmental disorders, overview. Importance of prenylation in synaptic function. GGTI not only regulates the basal neuronal dendritic growth but also mediates neuronal activity and BDNF-induced dendritogenesis. GGTI promotes neuronal dendritogenesis via increasing the membrane association of Rac1 in CNS neurons
both alpha and beta subunits are composed primarily of alpha helices. The beta subunits of GGTI consist of 13 alpha helices, and 12 of them are folded into an alpha-alpha barrel. The helices of the alpha subunit are arranged in a crescent-shaped superhelix that wraps around the alpha-alpha barrel of beta subunit. This arrangement creates a deep, funnel-shaped cavity in the center of the barrel, and the active sites of GGTI are located within this cavity
both alpha and beta subunits are composed primarily of alpha helices. The beta subunits of GGTI consist of 13 alpha helices, and 12 of them are folded into an alpha-alpha barrel. The helices of the alpha subunit are arranged in a crescent-shaped superhelix that wraps around the alpha-alpha barrel of beta subunit. This arrangement creates a deep, funnel-shaped cavity in the center of the barrel, and the active sites of GGTI are located within this cavity
both alpha and beta subunits are composed primarily of alpha helices. The beta subunits of GGTI consist of 13 alpha helices, and 12 of them are folded into an alpha-alpha barrel. The helices of the alpha subunit are arranged in a crescent-shaped superhelix that wraps around the alpha-alpha barrel of beta subunit. This arrangement creates a deep, funnel-shaped cavity in the center of the barrel, and the active sites of GGTI are located within this cavity
both alpha and beta subunits are composed primarily of alpha helices. The beta subunits of GGTI consist of 13 alpha helices, and 12 of them are folded into an alpha-alpha barrel. The helices of the alpha subunit are arranged in a crescent-shaped superhelix that wraps around the alpha-alpha barrel of beta subunit. This arrangement creates a deep, funnel-shaped cavity in the center of the barrel, and the active sites of GGTI are located within this cavity