Polygalacturonase [Carbohydrate transport and metabolism].

Acetyltransferase (GNAT) family. This family contains proteins with N-acetyltransferase functions such as Elp3-related proteins.

Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal structure and biogenesis].

N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer of an acyl group to a substrate. NAT (N-Acyltransferase) is a large superfamily of enzymes that mostly catalyze the transfer of an acyl group to a substrate and are implicated in a variety of functions, ranging from bacterial antibiotic resistance to circadian rhythms in mammals. Members include GCN5-related N-Acetyltransferases (GNAT) such as Aminoglycoside N-acetyltransferases, Histone N-acetyltransferase (HAT) enzymes, and Serotonin N-acetyltransferase, which catalyze the transfer of an acetyl group to a substrate. The kinetic mechanism of most GNATs involves the ordered formation of a ternary complex: the reaction begins with Acetyl Coenzyme A (AcCoA) binding, followed by binding of substrate, then direct transfer of the acetyl group from AcCoA to the substrate, followed by product and subsequent CoA release. Other family members include Arginine/ornithine N-succinyltransferase, Myristoyl-CoA: protein N-myristoyltransferase, and Acyl-homoserinelactone synthase which have a similar catalytic mechanism but differ in types of acyl groups transferred. Leucyl/phenylalanyl-tRNA-protein transferase and FemXAB nonribosomal peptidyltransferases which catalyze similar peptidyltransferase reactions are also included.

Acetyltransferase (GNAT) domain. This domain catalyzes N-acetyltransferase reactions.

Thecrystal structure of a hyperthermoactive Exopolygalacturonase from Thermotoga maritima [Thermotoga maritima],3JUR_B The crystal structure of a hyperthermoactive Exopolygalacturonase from Thermotoga maritima [Thermotoga maritima],3JUR_C The crystal structure of a hyperthermoactive Exopolygalacturonase from Thermotoga maritima [Thermotoga maritima],3JUR_D The crystal structure of a hyperthermoactive Exopolygalacturonase from Thermotoga maritima [Thermotoga maritima]

Crystalstructure of a putative glycosyl hydrolase (PARMER_00599) from Parabacteroides merdae ATCC 43184 at 1.95 A resolution [Parabacteroides merdae ATCC 43184],4MXN_B Crystal structure of a putative glycosyl hydrolase (PARMER_00599) from Parabacteroides merdae ATCC 43184 at 1.95 A resolution [Parabacteroides merdae ATCC 43184],4MXN_C Crystal structure of a putative glycosyl hydrolase (PARMER_00599) from Parabacteroides merdae ATCC 43184 at 1.95 A resolution [Parabacteroides merdae ATCC 43184],4MXN_D Crystal structure of a putative glycosyl hydrolase (PARMER_00599) from Parabacteroides merdae ATCC 43184 at 1.95 A resolution [Parabacteroides merdae ATCC 43184]