Enzymes
| UniProtKB help_outline | 29,440 proteins |
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Name help_outline
(1,4-α-D-glucosyl)n
Identifier
CHEBI:15444
Charge
0
Formula
(C6H10O5)nH2O
Search links
Involved in 8 reaction(s)
Find proteins in UniProtKB for this molecule
Form(s) in this reaction:
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Identifier: RHEA-COMP:9584Polymer name: [(1→4)-α-D-glucosyl](n)Polymerization index help_outline nFormula H2O(C6H10O5)nCharge (0)(0)nMol File for the polymer
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Identifier: RHEA-COMP:9587Polymer name: [(1→4)-α-D-glucosyl](n+1)Polymerization index help_outline n+1Formula H2O(C6H10O5)n+1Charge (0)(0)n+1Mol File for the polymer
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- Name help_outline ADP-α-D-glucose Identifier CHEBI:57498 Charge -2 Formula C16H23N5O15P2 InChIKeyhelp_outline WFPZSXYXPSUOPY-ROYWQJLOSA-L SMILEShelp_outline Nc1ncnc2n(cnc12)[C@@H]1O[C@H](COP([O-])(=O)OP([O-])(=O)O[C@H]2O[C@H](CO)[C@@H](O)[C@H](O)[C@H]2O)[C@@H](O)[C@H]1O 2D coordinates Mol file for the small molecule Search links Involved in 10 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline ADP Identifier CHEBI:456216 (Beilstein: 3783669) help_outline Charge -3 Formula C10H12N5O10P2 InChIKeyhelp_outline XTWYTFMLZFPYCI-KQYNXXCUSA-K SMILEShelp_outline Nc1ncnc2n(cnc12)[C@@H]1O[C@H](COP([O-])(=O)OP([O-])([O-])=O)[C@@H](O)[C@H]1O 2D coordinates Mol file for the small molecule Search links Involved in 841 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline H+ Identifier CHEBI:15378 Charge 1 Formula H InChIKeyhelp_outline GPRLSGONYQIRFK-UHFFFAOYSA-N SMILEShelp_outline [H+] 2D coordinates Mol file for the small molecule Search links Involved in 9,431 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Cross-references
| RHEA:18189 | RHEA:18190 | RHEA:18191 | RHEA:18192 | |
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| Reaction direction help_outline | undefined | left-to-right | right-to-left | bidirectional |
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Related reactions help_outline
More general form(s) of this reaction
Publications
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Starch and oligosaccharide synthesis from uridine diphosphate glucose.
LELOIR L.F., DE FEKETE M.A., CARDINI C.E.
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Biosynthesis of glucans in mung bean seedlings. Formation of beta-(1,4)-glucans from GDP-glucose and beta-(1,3)-glucans from UDP-glucose.
Chambers J., Elbein A.D.
Arch Biochem Biophys 138:620-631(1970) [PubMed] [EuropePMC]
This publication is cited by 1 other entry.
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Study of two glycosyltransferases related to polysaccharide biosynthesis in <i>Rhodococcus jostii</i> RHA1.
Cereijo A.E., Ferretti M.V., Iglesias A.A., Alvarez H.M., Asencion Diez M.D.
The bacterial genus <i>Rhodococcus</i> comprises organisms performing oleaginous behaviors under certain growth conditions and ratios of carbon and nitrogen availability. <i>Rhodococci</i> are outstanding producers of biofuel precursors, where lipid and glycogen metabolisms are closely related. Th ... >> More
The bacterial genus <i>Rhodococcus</i> comprises organisms performing oleaginous behaviors under certain growth conditions and ratios of carbon and nitrogen availability. <i>Rhodococci</i> are outstanding producers of biofuel precursors, where lipid and glycogen metabolisms are closely related. Thus, a better understanding of rhodococcal carbon partitioning requires identifying catalytic steps redirecting sugar moieties to storage molecules. Here, we analyzed two GT4 glycosyl-transferases from <i>Rhodococcus jostii</i> (<i>Rjo</i>GlgAb and <i>Rjo</i>GlgAc) annotated as α-glucan-α-1,4-glucosyl transferases, putatively involved in glycogen synthesis. Both enzymes were produced in <i>Escherichia coli</i> cells, purified to homogeneity, and kinetically characterized. <i>Rjo</i>GlgAb and <i>Rjo</i>GlgAc presented the "canonical" glycogen synthase activity and were actives as maltose-1P synthases, although to a different extent. Then, <i>Rjo</i>GlgAc is a homologous enzyme to the mycobacterial GlgM, with similar kinetic behavior and glucosyl-donor preference. <i>Rjo</i>GlgAc was two orders of magnitude more efficient to glucosylate glucose-1P than glycogen, also using glucosamine-1P as a catalytically efficient aglycon. Instead, <i>Rjo</i>GlgAb exhibited both activities with similar kinetic efficiency and preference for short-branched α-1,4-glucans. Curiously, <i>Rjo</i>GlgAb presented a super-oligomeric conformation (higher than 15 subunits), representing a novel enzyme with a unique structure-to-function relationship. Kinetic results presented herein constitute a hint to infer on polysaccharides biosynthesis in <i>rhodococci</i> from an enzymological point of view. << Less
Biol Chem 405:325-340(2024) [PubMed] [EuropePMC]
This publication is cited by 1 other entry.
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STUDIES ON ADENOSINE DIPHOSPHATE D-GLUCOSE: ALPHA-1,4-GLUCAN ALPHA-4-GLUCOSYLTRANSFERASE OF SWEET-CORN ENDOSPERM.
FRYDMAN R.B., CARDINI C.E.
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BIOSYNTHESIS OF BACTERIAL GLYCOGEN. II. PURIFICATION AND PROPERTIES OF THE ADENOSINE DIPHOSPHOGLUCOSE:GLYCOGEN TRANSGLUCOSYLASE OF ARTHROBACTER SPECIES NRRL B1973.
GREENBERG E., PREISS J.