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2.7.7.9: UTP-glucose-1-phosphate uridylyltransferase

This is an abbreviated version!
For detailed information about UTP-glucose-1-phosphate uridylyltransferase, go to the full flat file.

Word Map on EC 2.7.7.9

Reaction

UTP
+
alpha-D-glucose 1-phosphate
=
diphosphate
 +
UDP-glucose

Synonyms

All3274, CugP, cyanobacterial UDP-Glc PPase, ExoN, GalU, gfugp, Glc-1-P UTase, GlcNAc-1-P UTase, glucose 1-phosphate uridylyltransferase, glucose-1-phosphate urididyltransferase, glucose-1-phosphate uridyltransferase, glucose-1-phosphate uridylyltransferase, KF278717, plastid UDP-glucose pyrophosphorylase, rml-1, ScUGPase-1, sll1558, ST0452, ST0452 protein, STK_04520, sugar-1-P NTase, sugar-1-phosphate nucleotidylyltransferase, TaGalU, UDP glucose pyrophosphorylase, UDP-Glc pyrophosphorylase, UDP-GlcPPase, UDP-glucose pyrophosphorylase, UDP-glucose pyrophosphorylase 1, UDP-glucose pyrophosphorylase isoenzyme UGP5, UDP-glucose pyrophosphorylase UGP1, UDP-glucose pyrophosphorylase UGP2, UDP-glucose pyrophosphorylase UGP3, UDPG phosphorylase, UDPG pyrophosphorylase, UDPG-pyrophosphorylase, UDPglucose pyrophosphorylase, UDPGP, UGP, ugp-1, UGP1, UGP3, UgpA, UGPase, UGPase1, UGPase2, UGPG-PPase, UPD1, uridine 5'-diphosphoglucose pyrophosphorylase, uridine diphosphate-D-glucose pyrophosphorylase, uridine diphosphate-glucose pyrophosphorylase, uridine diphosphoglucose pyrophosphorylase, uridine-diphosphate glucose pyrophosphorylase, uridylyltransferase, glucose 1-phosphate, UTP/dTTP-glucose-1-phosphate uridylyl/thymidylyl transferase, UTP:alpha-D-glucose uridylyltransferase, UTP:glucose-1-phosphate uridylyltransferase, VldB

ECTree

     2 Transferases
         2.7 Transferring phosphorus-containing groups
             2.7.7 Nucleotidyltransferases
                2.7.7.9 UTP-glucose-1-phosphate uridylyltransferase

Temperature Stability

Temperature Stability on EC 2.7.7.9 - UTP-glucose-1-phosphate uridylyltransferase

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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30 - 55
approximately 70% of the enzyme activity is maintained when the enzyme is incubated at 30°C to 55°C for 1 h
40
-
15 min, 10% loss of activity
47
-
t1/2: 10 min
52
-
30 min, 70% loss of activity, 0.25 M potassium phosphate buffer, pH 7.5-9.0
65
-
1 90% loss of activity
80
mutant enzyme DC005 shows the same thermostability as wild-type ST0452 protein, whereas mutant enzyme DC011 denatures and becomes insoluble form by 5-min treatment at 80 °C. The C-terminal domain of the ST0452 protein, with its LbetaH structure, appears to be essential for the formation of its trimeric form and, in turn, the high stability of the entire ST0452 protein
additional information
-
isozymes of different heat stability