Any feedback?
Please rate this page
(enzyme.php)
(0/150)

BRENDA support

BRENDA Home
show all | hide all No of entries

Information on EC 2.7.7.13 - mannose-1-phosphate guanylyltransferase and Organism(s) Homo sapiens

for references in articles please use BRENDA:EC2.7.7.13
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
IUBMB Comments
The bacterial enzyme can also use ITP and dGTP as donors.
Specify your search results
Select one or more organisms in this record: ?
This record set is specific for:
Homo sapiens
Show additional data
Do not include text mining results
Include (text mining) results
Include results (AMENDA + additional results, but less precise)
Word Map
The taxonomic range for the selected organisms is: Homo sapiens
The enzyme appears in selected viruses and cellular organisms
Synonyms
gmppb, gdp-mannose pyrophosphorylase, vtc1-1, gdp-d-mannose pyrophosphorylase, gdp-mp, osvtc1-1, osvtc1-3, nspase, mannose-1-phosphate guanylyltransferase, gdp-man pyrophosphorylase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
GDP-mannose pyrophosphorylase
GDP-mannose pyrophosphorylase B
-
GDP-MP
-
-
GTP-mannose 1-phosphate guanylyltransferase
-
-
-
-
GTP-mannose-1-phosphate guanylyltransferase
-
-
-
-
guanosine 5'-diphospho-D-mannose pyrophosphorylase
-
-
-
-
guanosine diphosphate mannose pyrophosphorylase
-
guanosine diphosphate mannose pyrophosphorylase B
-
guanosine diphosphomannose pyrophosphorylase
-
-
-
-
guanosine triphosphate-mannose 1-phosphate guanylyltransferase
-
-
-
-
guanylyltransferase, mannose 1-phosphate
-
-
-
-
mannose 1-phosphate guanylyltransferase (guanosine triphosphate)
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
nucleotidyl group transfer
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
GTP:alpha-D-mannose-1-phosphate guanylyltransferase
The bacterial enzyme can also use ITP and dGTP as donors.
CAS REGISTRY NUMBER
COMMENTARY hide
37278-24-3
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
GTP + alpha-D-mannose 1-phosphate
diphosphate + GDP-alpha-D-mannose
show the reaction diagram
-
-
-
?
GTP + alpha-D-mannose 1-phosphate
diphosphate + GDP-mannose
show the reaction diagram
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
GTP + alpha-D-mannose 1-phosphate
diphosphate + GDP-mannose
show the reaction diagram
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Mg2+
-
required
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
4-[4-[(4-tert-butylphenyl)methyl]piperazin-1-yl]-7-chloroquinoline
-
competitive inhibitor
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.02
4-[4-[(4-tert-butylphenyl)methyl]piperazin-1-yl]-7-chloroquinoline
Homo sapiens
-
pH and temperature not specified in the publication
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
enzyme deficiency leads to reduced alpha-dystroglycan glycosylation in the muscle biopsies of affected individuals and in available fibroblasts. Mutations in GDP-mannose pyrophosphorylase B (GMPPB) can result in muscular dystrophy variants with hypoglycosylated alpha-dystroglycan. Overexpression of wild-type GMPPB in fibroblasts from an affected individual partially restores glycosylation of alpha-dystroglycan in muscle. Five of the identified missense mutations cause formation of aggregates in the cytoplasm or near membrane protrusions. Enzyme mutant phenotypes with brain and muscle abnormalities, overview
physiological function
the enzyme catalyzes the formation of GDP-mannose from GTP and mannose-1-phosphate. GDP-mannose is required for O-mannosylation of proteins, including alpha-dystroglycan, and it is the substrate of cytosolic mannosyltransferases
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
GMPPB_HUMAN
360
0
39834
Swiss-Prot
Mitochondrion (Reliability: 3)
A0A7I2YQI5_HUMAN
396
0
43895
TrEMBL
Mitochondrion (Reliability: 3)
A0A024R329_HUMAN
387
0
42622
TrEMBL
Mitochondrion (Reliability: 3)
A0A7I2V4B5_HUMAN
255
0
27975
TrEMBL
Mitochondrion (Reliability: 3)
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hexamer
-
-
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
comparison of structural models of the GDP-mannose diphosphorylases from human and Leishmania donovani. The human active site is site very similar to the Leishmania donovani one. Leishmania donovani GDP-mannose diphosphorylase makes more interactions with its substrate than the human enzyme does
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D27H/V330I
mutation identified in patient with muscular dystrophy
P22S/D334N
mutation identified in patient with muscular dystrophy
P32L
mutation identified in patient with muscular dystrophy
P32L/R287Q
mutation identified in patient with muscular dystrophy
R185C
mutation identified in patient with muscular dystrophy
R287Q
mutation identified in patient with muscular dystrophy
R74*/D334N
mutation identified in patient with muscular dystrophy
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
medicine
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Carss, K.J.; Stevens, E.; Foley, A.R.; Cirak, S.; Riemersma, M.; Torelli, S.; Hoischen, A.; Willer, T.; van Scherpenzeel, M.; Moore, S.A.; Messina, S.; Bertini, E.; Boennemann, C.G.; Abdenur, J.E.; Grosmann, C.M.; Kesari, A.; Punetha, J.; Quinlivan, R.; Waddell, L.B.; Young, H.K.; Wraige, E.; Yau, S.; Bro, L. et al.
Mutations in GDP-mannose pyrophosphorylase B cause congenital and limb-girdle muscular dystrophies associated with hypoglycosylation of alpha-dystroglycan
Am. J. Hum. Genet.
93
29-41
2013
Danio rerio (Q6DBU5), Danio rerio, Homo sapiens (Q9Y5P6)
Manually annotated by BRENDA team
Daligaux, P.; Bernadat, G.; Tran, L.; Cave, C.; Loiseau, P.; Pomel, S.; Ha-Duong, T.
Comparative study of structural models of Leishmania donovani and human GDP-mannose pyrophosphorylases
Eur. J. Med. Chem.
107
109-118
2016
Leishmania donovani (E9BG32), Homo sapiens (Q9Y5P6), Leishmania donovani BPK282A1 (E9BG32)
Manually annotated by BRENDA team
Carss, K.J.; Stevens, E.; Foley, A.R.; Cirak, S.; Riemersma, M.; Torelli, S.; Hoischen, A.; Willer, T.; van Scherpenzeel, M.; Moore, S.A.; Messina, S.; Bertini, E.; Boennemann, C.G.; Abdenur, J.E.; Grosmann, C.M.; Kesari, A.; Punetha, J.; Quinlivan, R.; Waddell, L.B.; Young, H.K.; Wraige, E.; Yau, S.; et, al.
Mutations in GDP-mannose pyrophosphorylase B cause congenital and limb-girdle muscular dystrophies associated with hypoglycosylation of alpha-dystroglycan
Am. J. Hum. Genet.
93
29-41
2013
Homo sapiens (Q9Y5P6)
Manually annotated by BRENDA team
Pomel, S.; Mao, W.; Ha-Duong, T.; Cave, C.; Loiseau, P.
GDP-mannose pyrophosphorylase A biologically validated target for drug development against leishmaniasis
Front. Cell. Infect. Microbiol.
9
186
2019
Homo sapiens, Leishmania donovani, Leishmania mexicana
Manually annotated by BRENDA team