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Information on EC 5.4.99.16 - maltose alpha-D-glucosyltransferase and Organism(s) Mycobacterium tuberculosis and UniProt Accession P9WQ19

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EC Tree
     5 Isomerases
         5.4 Intramolecular transferases
             5.4.99 Transferring other groups
                5.4.99.16 maltose alpha-D-glucosyltransferase
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Mycobacterium tuberculosis
UNIPROT: P9WQ19 not found.
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Word Map
The taxonomic range for the selected organisms is: Mycobacterium tuberculosis
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
Synonyms
mtase, trehalose synthase, tttres, trehalose synthetase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
57-KDa trehalose synthase (Saccharomyces cerevisiae)
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Maltose alpha-D-glucosylmutase
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Maltose alpha-D-glucosyltransferase
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Maltose glucosylmutase
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Protein (Saccharomyces cerevisiae clone pMB14 gene CIF reduced)
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Protein (Saccharomyces cerevisiae gene CIF1 reduced)
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Synthase, trehalose
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Synthase, trehalose (Pimelobacter strain R48 clone pBRM8 gene treS precursor reduced)
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Synthase, trehalose (Saccharomyces cerevisiae gene TPS1 subunit)
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Synthase, trehalose (Saccharomyces cerevisiae gene TSL1 subunit)
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Synthase, trehalose (Thermus aquaticus strain ATCC33923 clone pBTM5)
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Trehalose synthase
Trehalose synthase (Pimelobacter strain R48 clone pBRM8 gene treS precursor reduced)
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Trehalose synthetase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
maltose = alpha,alpha-trehalose
show the reaction diagram
two-step, double displacement mechanism of the enzyme, overview
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
glycosyl bond isomerization
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PATHWAY SOURCE
PATHWAYS
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SYSTEMATIC NAME
IUBMB Comments
maltose alpha-D-glucosylmutase
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CAS REGISTRY NUMBER
COMMENTARY hide
147994-22-7
protein (Saccharomyces cerevisiae clone pMB14 gene CIF reduced) /57-KDa trehalose synthase (Saccharomyces cerevisiae gene CIF1) /protein (Saccharomyces cerevisiae gene CIF1 reduced) /synthase, trehalose (Saccharomyces cerevisiae gene TPS1 subunit)
178604-93-8
synthase, trehalose (Pimelobacter strain R48 clone pBRM8 gene treS precursor reduced) /trehalose synthase (Pimelobacter strain R48 clone pBRM8 gene treS precursor reduced)
187285-67-2
synthase, trehalose (Thermus aquaticus strain ATCC33923 clone pBTM5)
211621-92-0
synthase, trehalose (Saccharomyces cerevisiae gene TSL1 subunit)
395644-91-4
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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
maltose
alpha,alpha-trehalose
show the reaction diagram
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r
maltose
alpha,alpha-trehalose
show the reaction diagram
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r
additional information
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TreS has also amylase activity by producing trehalose from glycogen or maltoheptaose
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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
maltose
alpha,alpha-trehalose
show the reaction diagram
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r
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Ca2+
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the MTase activity of TreS is inhibited by 5 mM Ca2+ and other divalent cations
validoxylamine
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strong inhibition
additional information
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not inhibited by acarbose
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
390000
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gel filtration
65000
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6 * 65000, SDS-PAGE
68000
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6 * 68000, gel filtration
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homohexamer
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
enzyme complexed with Ca2+, glycerin, and sulfate ion, PDB ID 4LXF, X-ray diffraction structure determination and analysis at 2.6 A resolution
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
Ni column chromatography
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
physicochemical properties and industrial applications of trehalose, overview. The low energy (<1 kcal/mol) of the alpha,alpha-1,1-glycosidic bond enables trehalose to be the most stable sugar in solutions. In cosmetics, trehalose is in creams and lotions as moisture-retaining agent and storage stability enhancer and suppressor of the odor from active ingredients. In pharmaceuticals, trehalose has had roles in the preservation of tissues and organs for transplantation and cryopreservation of blood stem cells and sperm, with increased cell viability. Trehalose is also reported to have a suppression effect on bone loss. In vivo studies showed trehalose is found to be effective in reducing peptide aggregation and increasing autophagy in animal models of neurodegenerative disorders including Alzheimer's disease, Parkinson's disease, and Huntington's disease
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Pan, Y.T.; Carroll, J.D.; Asano, N.; Pastuszak, I.; Edavana, V.K.; Elbein, A.D.
Trehalose synthase converts glycogen to trehalose
FEBS J.
275
3408-3420
2008
Mycobacterium tuberculosis, Mycolicibacterium smegmatis
Manually annotated by BRENDA team
Cai, X.; Seitl, I.; Mu, W.; Zhang, T.; Stressler, T.; Fischer, L.; Jiang, B.
Biotechnical production of trehalose through the trehalose synthase pathway current status and future prospects
Appl. Microbiol. Biotechnol.
102
2965-2976
2018
Corynebacterium glutamicum (A0A1R4FYB1), Corynebacterium glutamicum ATCC 13032 (A0A1R4FYB1), Deinococcus geothermalis (Q1J0Z5), Deinococcus geothermalis DSMZ 11300 (Q1J0Z5), Deinococcus radiodurans (I3NX86), Deinococcus radiodurans (Q9RST7), Deinococcus radiodurans ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB 9279 / R1 / VKM B-1422 (I3NX86), Deinococcus radiodurans ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB 9279 / R1 / VKM B-1422 (Q9RST7), Enterobacter hormaechei (F5S1H2), Enterobacter hormaechei ATCC 49162 (F5S1H2), Meiothermus ruber (B1PK99), Mycobacterium tuberculosis (P9WQ19), Mycobacterium tuberculosis ATCC 25618 / H37Rv (P9WQ19), Mycolicibacterium smegmatis (A0R6E0), Mycolicibacterium smegmatis ATCC 700084 / mc2_155 (A0R6E0), Paenarthrobacter aurescens (B8YM30), Picrophilus torridus (Q6L2Z7), Picrophilus torridus DSM 9790 (Q6L2Z7), Pseudomonas sp. P8005 (I3WCP4), Pseudomonas stutzeri (A0A4S2BJW1), Pseudomonas stutzeri CJ38 (A0A4S2BJW1), Rhodococcus opacus (M1PA89), Rhodococcus opacus ATCC 41021 (M1PA89), Thermobaculum terrenum (D1CE96), Thermobifida fusca (Q47SE5), Thermobifida fusca DSM 43792 (Q47SE5), Thermomonospora curvata (D1ABU6), Thermomonospora curvata DSM 43183 (D1ABU6), Thermus thermophilus, Thermus thermophilus (O06458), Thermus thermophilus ATCC 33923 (O06458)
Manually annotated by BRENDA team