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Literature summary for 2.7.7.27 extracted from

  • Georgelis, N.; Shaw, J.R.; Hannah, L.C.
    Phylogenetic analysis of ADP-glucose pyrophosphorylase subunits reveals a role of subunit interfaces in the allosteric properties of the enzyme (2009), Plant Physiol., 151, 67-77.
    View publication on PubMedView publication on EuropePMC

Activating Compound

Activating Compound Comment Organism Structure
3-phosphoglycerate 3-PGA Solanum tuberosum
3-phosphoglycerate 3-PGA Zea mays

Cloned(Commentary)

Cloned (Comment) Organism
for expression in Escherichia coli AC70R1-504 cells Zea mays

Protein Variants

Protein Variants Comment Organism
A508S large subunit mutation Zea mays
C114A large subunit mutation Zea mays
C382F large subunit mutation Zea mays
C424V large subunit mutation Zea mays
D368S large subunit mutation Zea mays
E438Q large subunit mutation Zea mays
H149S large subunit mutation Zea mays
M172T large subunit mutation Zea mays
P372A large subunit mutation Zea mays
Q213H large subunit mutation Zea mays
S163F large subunit mutation Zea mays
T361C large subunit mutation Zea mays
V227R large subunit mutation Zea mays
V502T large subunit mutation Zea mays

Inhibitors

Inhibitors Comment Organism Structure
inorganic phosphate
-
Solanum tuberosum
phosphate
-
Zea mays

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.05
-
alpha-D-glucose 1-phosphate mutant BT2/E438Q Zea mays
0.05
-
alpha-D-glucose 1-phosphate mutant BT2/P372A Zea mays
0.06
-
alpha-D-glucose 1-phosphate mutant BT2/A508S Zea mays
0.06
-
alpha-D-glucose 1-phosphate mutant BT2/M172T Zea mays
0.06
-
alpha-D-glucose 1-phosphate mutant BT2/T361C Zea mays
0.06
-
alpha-D-glucose 1-phosphate mutant BT2/V227R Zea mays
0.06
-
alpha-D-glucose 1-phosphate mutant BT2/V502T Zea mays
0.07
-
alpha-D-glucose 1-phosphate mutant BT2/C114A Zea mays
0.07
-
alpha-D-glucose 1-phosphate mutant BT2/D368S Zea mays
0.07
-
alpha-D-glucose 1-phosphate mutant BT2/H149S Zea mays
0.07
-
alpha-D-glucose 1-phosphate mutant BT2/Q213H Zea mays
0.07
-
alpha-D-glucose 1-phosphate wild type BT2/SH2 Zea mays
0.08
-
alpha-D-glucose 1-phosphate mutant BT2/C382F Zea mays
0.09
-
ATP mutant BT2/A508S Zea mays
0.09
-
alpha-D-glucose 1-phosphate mutant BT2/C424V Zea mays
0.09
-
ATP mutant BT2/M172T Zea mays
0.09
-
alpha-D-glucose 1-phosphate mutant BT2/S163F Zea mays
0.11
-
ATP mutant BT2/D368S Zea mays
0.12
-
ATP wild type BT2/SH2 Zea mays
0.13
-
ATP mutant BT2/E438Q Zea mays
0.13
-
ATP mutant BT2/T361C Zea mays
0.14
-
ATP mutant BT2/C114A Zea mays
0.14
-
ATP mutant BT2/C424V Zea mays
0.14
-
ATP mutant BT2/V227R Zea mays
0.15
-
ATP mutant BT2/C382F Zea mays
0.15
-
ATP mutant BT2/V502T Zea mays
0.19
-
ATP mutant BT2/H149S Zea mays
0.19
-
ATP mutant BT2/P372A Zea mays
0.21
-
ATP mutant BT2/Q213H Zea mays
0.42
-
ATP mutant BT2/S163F Zea mays

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
ATP + alpha-D-glucose 1-phosphate Solanum tuberosum
-
diphosphate + ADP-glucose
-
?
ATP + alpha-D-glucose 1-phosphate Zea mays
-
diphosphate + ADP-glucose
-
?

Organism

Organism UniProt Comment Textmining
Solanum tuberosum Q00081 fragment
-
Zea mays P55241
-
-

Purification (Commentary)

Purification (Comment) Organism
by protamine sulfate and ammonium sulfate fractionation, followed by anion-exchange and affinity chromatography Zea mays

Source Tissue

Source Tissue Comment Organism Textmining
endosperm
-
Zea mays
-
tuber
-
Solanum tuberosum
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + alpha-D-glucose 1-phosphate
-
Solanum tuberosum diphosphate + ADP-glucose
-
?
ATP + alpha-D-glucose 1-phosphate
-
Zea mays diphosphate + ADP-glucose
-
?

Subunits

Subunits Comment Organism
heterotetramer consists of two small and two large subunits Solanum tuberosum
heterotetramer consists of two small and two large subunits, BT2/SH2 Zea mays

Synonyms

Synonyms Comment Organism
ADP-glucose pyrophosphorylase
-
Solanum tuberosum
ADP-glucose pyrophosphorylase
-
Zea mays
AGPase
-
Solanum tuberosum
AGPase
-
Zea mays
BT2 maize AGPase endosperm small subunit Zea mays
SH2 maize AGPase endosperm large subunit Zea mays

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
activity assay Zea mays

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
16.17
-
alpha-D-glucose 1-phosphate mutant BT2/V227R Zea mays
23.34
-
alpha-D-glucose 1-phosphate mutant BT2/D368S Zea mays
29.36
-
alpha-D-glucose 1-phosphate mutant BT2/Q213H Zea mays
32.87
-
alpha-D-glucose 1-phosphate mutant BT2/E438Q Zea mays
34.65
-
alpha-D-glucose 1-phosphate mutant BT2/S163F Zea mays
35.21
-
alpha-D-glucose 1-phosphate mutant BT2/H149S Zea mays
35.77
-
alpha-D-glucose 1-phosphate mutant BT2/A508S Zea mays
37.21
-
alpha-D-glucose 1-phosphate mutant BT2/C114A Zea mays
38.12
-
alpha-D-glucose 1-phosphate mutant BT2/T361C Zea mays
38.58
-
alpha-D-glucose 1-phosphate mutant BT2/M172T Zea mays
39.17
-
alpha-D-glucose 1-phosphate wild type BT2/SH2 Zea mays
40.75
-
alpha-D-glucose 1-phosphate mutant BT2/C382F Zea mays
41.91
-
alpha-D-glucose 1-phosphate mutant BT2/V502T Zea mays
42.32
-
alpha-D-glucose 1-phosphate mutant BT2/P372A Zea mays
59.86
-
alpha-D-glucose 1-phosphate mutant BT2/C424V Zea mays

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.4
-
activity assay Zea mays

Cofactor

Cofactor Comment Organism Structure
ATP
-
Solanum tuberosum
ATP
-
Zea mays

Ki Value [mM]

Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
1.83
-
phosphate mutant BT2/S163F, 15 mM 3-phosphoglycerate Zea mays
2.28
-
phosphate mutant BT2/C382F, 15 mM 3-phosphoglycerate Zea mays
3.21
-
phosphate mutant BT2/Q213H, 15 mM 3-phosphoglycerate Zea mays
3.72
-
phosphate mutant BT2/P372A, 15 mM 3-phosphoglycerate Zea mays
3.96
-
phosphate mutant BT2/H149S, 15 mM 3-phosphoglycerate Zea mays
4.26
-
phosphate mutant BT2/D368S, 15 mM 3-phosphoglycerate Zea mays
5.34
-
phosphate mutant BT2/T361C, 15 mM 3-phosphoglycerate Zea mays
13.23
-
phosphate mutant BT2/C114A, 15 mM 3-phosphoglycerate Zea mays
14.5
-
phosphate mutant BT2/V227R, 15 mM 3-phosphoglycerate Zea mays
15.22
-
phosphate mutant BT2/E438Q, 15 mM 3-phosphoglycerate Zea mays
16.8
-
phosphate wild type BT2/SH2, 15 mM 3-phosphoglycerate Zea mays
17.61
-
phosphate mutant BT2/M172T, 15 mM 3-phosphoglycerate Zea mays
17.93
-
phosphate mutant BT2/V502T, 15 mM 3-phosphoglycerate Zea mays
18.36
-
phosphate mutant BT2/C424V, 15 mM 3-phosphoglycerate Zea mays
20.43
-
phosphate mutant BT2/A508S, 15 mM 3-phosphoglycerate Zea mays

General Information

General Information Comment Organism
physiological function ADP-glucose pyrophosphorylase catalyzes the rate-limiting step in starch biosynthesis Solanum tuberosum
physiological function ADP-glucose pyrophosphorylase catalyzes the rate-limiting step in starch biosynthesis Zea mays