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Information on EC 2.4.1.66 - procollagen glucosyltransferase and Organism(s) Mus musculus and UniProt Accession Q9R0E1

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EC Tree
     2 Transferases
         2.4 Glycosyltransferases
             2.4.1 Hexosyltransferases
                2.4.1.66 procollagen glucosyltransferase
IUBMB Comments
Involved in the synthesis of carbohydrate units in the complement system (cf. EC 2.4.1.50 procollagen galactosyltransferase).
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This record set is specific for:
Mus musculus
UNIPROT: Q9R0E1
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Word Map
The taxonomic range for the selected organisms is: Mus musculus
The enzyme appears in selected viruses and cellular organisms
Synonyms
galactosylhydroxylysyl glucosyltransferase, collagen glucosyltransferase, galactosylhydroxylysine glucosyltransferase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
collagen glucosyltransferase
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collagen hydroxylysyl glucosyltransferase
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galactosylhydroxylysine glucosyltransferase
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galactosylhydroxylysyl glucosyltransferase
GGT
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glucosyltransferase, uridine diphosphoglucose-collagen
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lysyl hydroxylase 3
PLOD3
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UDP-glucose-collagen glucosyltransferase
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UDP-glucose:galactosylhydroxylysine-collagen glucosyltransferase
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uridine diphosphoglucose-collagen glucosyltransferase
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additional information
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hexosyl group transfer
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PATHWAY SOURCE
PATHWAYS
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SYSTEMATIC NAME
IUBMB Comments
UDP-glucose:(2S,5R)-5-O-(beta-D-galactosyl)-5-hydroxy-L-lysine-[procollagen] D-glucosyltransferase
Involved in the synthesis of carbohydrate units in the complement system (cf. EC 2.4.1.50 procollagen galactosyltransferase).
CAS REGISTRY NUMBER
COMMENTARY hide
9028-08-4
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
UDP-alpha-D-glucose + galactosylhydroxylysyl residues in a calf skin gelatin
UDP + glucosylgalactosylhydroxylysyl residues in a calf skin gelatin
show the reaction diagram
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?
UDP-glucose + 5-(D-galactosyloxy)-L-lysine-procollagen
UDP + 1,2-D-glucosyl-5-D-(galactosyloxy)-L-lysine-procollagen
show the reaction diagram
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?
additional information
?
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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
additional information
?
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the reduction of the galactosylhydroxylysyl glucosyltransferase activity of LH3 disrupts the localization of type IV collagen, and thus the formation of basement membranes during mouse embryogenesis leading to lethality at embryonic day 9.5-14.5. Survival of hypomorphic embryos and the formation of the basement membrane are directly correlated with the level of galactosylhydroxylysyl glucosyltransferase activity. An LH3-knockout mouse lacks galactosylhydroxylysyl glucosyltransferase. Lysyl hydroxylase 3 is the main molecule responsible for galactosylhydroxylysyl glucosyltransferase activity. Galactosylhydroxylysyl glucosyltransferase is essential for the formation of the basement membrane
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?
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
LH3 gene Plod3 with LH and GGT activity
SwissProt
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
RNA isolation from
Manually annotated by BRENDA team
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in kidney the enzyme is located mainly intracellularly
Manually annotated by BRENDA team
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the enzyme is located solely in the extracellular space
Manually annotated by BRENDA team
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Manually annotated by BRENDA team
additional information
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the reduction of the galactosylhydroxylysyl glucosyltransferase activity of LH3 disrupts the localization of type IV collagen, and thus the formation of basement membranes during mouse embryogenesis leading to lethality at embryonic day 9.5-14.5. Survival of hypomorphic embryos and the formation of the basement membrane are directly correlated with the level of galactosylhydroxylysyl glucosyltransferase activity. An LH3-knockout mouse lacks galactosylhydroxylysyl glucosyltransferase. Lysyl hydroxylase 3 is the main molecule responsible for galactosylhydroxylysyl glucosyltransferase activity. Galactosylhydroxylysyl glucosyltransferase is essential for the formation of the basement membrane
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
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liver enzyme
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Manually annotated by BRENDA team
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kidney enzyme
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
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an impairment of lysyl hydroxylase 3 function significantly affects type I collagen fibrillogenesis
physiological function
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
PLOD3_MOUSE
741
0
84922
Swiss-Prot
Secretory Pathway (Reliability: 1)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
96000
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x * 96000, LH3-V5/His fusion protein, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
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x * 96000, LH3-V5/His fusion protein, SDS-PAGE
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
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MEF+/-, lysyl hydroxylase 3 knock-out mice, only 80% GGT activity in cell lysate, only 5% GGT activity in the culture medium
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
LH3-V5/His fusion protein is purified using nickel-nitrilotriacetic acid-agarose resin column chromatography
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
Plod3 gene encoding LH3/GGT is cloned and sequenced, gene structure and regulation, localized on chromosome 5
LH3-V5/His fusion protein is expressed in HEK-293 cells
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
decrease in lysyl hydroxylase 3 in LH3 knock-out mice
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Ruotsalainen, H.; Vanhatupa, S.; Tampio, M.; Sipil, L.; Valtavaara, M.; Myllyl, R.
Complete genomic structure of mouse lysyl hydroxylase 2 and lysyl hydroxylase 3/collagen glucosyltransferase
Matrix Biol.
20
137-146
2001
Mus musculus (Q9R0E1), Mus musculus
Manually annotated by BRENDA team
Ruotsalainen, H.; Sipilae, L.; Vapola, M.; Sormunen, R.; Salo, A.M.; Uitto, L.; Mercer, D.K.; Robins, S.P.; Risteli, M.; Aszodi, A.; Faessler, R.; Myllylae, R.
Glycosylation catalyzed by lysyl hydroxylase 3 is essential for basement membranes
J. Cell Sci.
119
625-635
2006
Mus musculus
Manually annotated by BRENDA team
Salo, A.M.; Wang, C.; Sipilae, L.; Sormunen, R.; Vapola, M.; Kervinen, P.; Ruotsalainen, H.; Heikkinen, J.; Myllylae, R.
Lysyl hydroxylase 3 (LH3) modifies proteins in the extracellular space, a novel mechanism for matrix remodeling
J. Cell. Physiol.
207
644-653
2006
Mus musculus
Manually annotated by BRENDA team
Risteli, M.; Ruotsalainen, H.; Salo, A.M.; Sormunen, R.; Sipilae, L.; Baker, N.L.; Lamande, S.R.; Vimpari-Kauppinen, L.; Myllylae, R.
Reduction of lysyl hydroxylase 3 causes deleterious changes in the deposition and organization of extracellular matrix
J. Biol. Chem.
284
28204-28211
2009
Homo sapiens (O60568), Mus musculus
Manually annotated by BRENDA team
Sricholpech, M.; Perdivara, I.; Yokoyama, M.; Nagaoka, H.; Terajima, M.; Tomer, K.B.; Yamauchi, M.
Lysyl hydroxylase 3-mediated glucosylation in type I collagen: molecular loci and biological significance
J. Biol. Chem.
287
22998-23009
2012
Homo sapiens, Mus musculus
Manually annotated by BRENDA team