1 sing galactokinase and galactose-1-phosphate uridyltransferase.

2 y KPAP1 poly(A) polymerase and RET1 terminal uridyltransferase.

3 otein that lacks the RNA-binding domains and uridyltransferase activity of the full protein.

4 tose concentrations in galactose-1-phosphate uridyltransferase-deficient patients suggest that other

5 struct with point mutations inactivating the uridyltransferase domain enhanced cell proliferation as

6 ere tested for their recognition by the GlmU uridyltransferase enzyme.

7  the function of human galactose-1-phosphate uridyltransferase (GALT) and is the most common mutation

8 g and 50% reduction in galactose-1-phosphate uridyltransferase (GALT) enzyme activity.

9      Deficiency in the galactose-1-phosphate uridyltransferase (GALT) enzyme results in accumulation

10 humans, the absence of galactose-1-phosphate uridyltransferase (GALT) leads to significant neonatal m

11 I results from loss of galactose-1-phosphate uridyltransferase (GALT), which converts galactose-1-pho

12                  N-Acetylglucosamine-1-PO(4) uridyltransferase (GlmU) is a trimeric bifunctional enzy

13 ly pyrophosphorylated by N-acetylglucosamine uridyltransferase (GlmU) to give UDP-GlcNAc/GalNAc.

14             N-acetyl-glucosamine-1-phosphate uridyltransferase (GlmU), a bifunctional enzyme involved

15 ase (PgcA) and UTP:alpha-glucose 1-phosphate uridyltransferase (GtaB) homologs are required for the s

16                                 Zcchc11 is a uridyltransferase protein with enzymatic activity direct

17  (MtbGlmU), a bifunctional acetyltransferase/uridyltransferase that catalyzes the formation of uridin

18                             Several terminal uridyltransferases (TUTases) are known to modulate small

19                                     Terminal uridyltransferases (TUTases) execute 3' RNA uridylation