Bacterial trehalose synthesis from alpha-glucans and maltose

A reusable bacterial module covering two alternative routes that form trehalose from alpha-glucosides. In the coupled TreY-TreZ route, TreY rearranges the reducing-end linkage of an alpha-1,4-glucan to form maltooligosyltrehalose and TreZ hydrolytically releases trehalose. In the standalone TreS route, one enzyme reversibly interconverts maltose and trehalose. Trehalose synthesis from nucleotide sugars, trehalose degradation, and upstream alpha-glucan or maltose supply are outside the boundary.

MODULE:bacterial_trehalose_synthesis_from_alpha_glucansDRAFTCONCRETEMetabolic Pathwaymodules/bacterial_trehalose_synthesis_from_alpha_glucans.yaml
trehalose biosynthetic processGO:0005992
PMID:8605217
Cloning and sequencing of trehalose biosynthesis genes from Arthrobacter sp. Q36.
The characterized Arthrobacter locus contains adjacent treY and treZ genes encoding the two reactions of the alpha-glucan route.
Sequence analysis of the DNA fragment revealed two open reading frames of 2325 and 1794 bp, encoding maltooligosyltrehalose synthase (TreY) and maltooligosyltrehalose trehalohydrolase (TreZ), respectively.
PMID:8611744
Purification and properties of a novel enzyme, maltooligosyl trehalose synthase, from Arthrobacter sp. Q36.
Purified Arthrobacter sp. Q36 TreY catalyzes the first route reaction.
Arthrobacter sp. Q36 produces a novel enzyme, maltooligosyl trehalose synthase, which catalyzes the conversion of maltooligosaccharide into the non-reducing saccharide, maltooligosyl trehalose (alpha-maltooligosyl alpha-D-glucoside) by intramolecular transglycosylation.
PMID:8611745
Purification and characterization of a novel enzyme, maltooligosyl trehalose trehalohydrolase, from Arthrobacter sp. Q36.
Purified Arthrobacter sp. Q36 TreZ catalyzes the second route reaction.
The enzyme specifically catalyzed the hydrolysis of the alpha-1,4-glucosidic linkage that bound the maltooligosyl and trehalose moieties of maltooligosyl trehalose.
PMID:25204684
Cloning and expression of a trehalose synthase from Pseudomonas putida KT2440 for the scale-up production of trehalose from maltose.
Recombinant Pseudomonas putida KT2440 TreS converted maltose to trehalose, directly supporting the standalone route in this strain.
High-pressure liquid chromatography results indicated that this enzyme had the ability to catalyze 59% maltose into trehalose, with about 5.1% glucose as by-product.
PMID:15654636
Cloning and expression of a trehalose synthase from Pseudomonas stutzeri CJ38 in Escherichia coli for the production of trehalose.
The characterized Pseudomonas stutzeri CJ38 TreS reversibly interconverts maltose and trehalose and supports the trehalose-forming direction represented by the standalone route.
Activity analysis, using either maltose or trehalose as a substrate, showed a reversible reaction.
UniProtKB:Q88FN6
Pseudomonas putida KT2440 TreY
Q88FN6 is the exact KT2440 TreY exemplar.
UniProtKB:Q88FN8
Pseudomonas putida KT2440 TreZ
Q88FN8 is the exact KT2440 TreZ exemplar.
UniProtKB:Q88IT1
Pseudomonas putida KT2440 TreSA
Q88IT1 is the standalone KT2440 TreS exemplar; its sequence begins with the peptide encoded by the cloning primer reported for the assayed KT2440 enzyme.
UniProtKB:Q9LAS5
Pseudomonas stutzeri CJ38 TreS
Q9LAS5 maps to GenBank AAF26837.1, the 689-residue CJ38 TreS characterized in PMID:15654636, and is a TIGR02455 TreS_stutzeri family member.

The TreY-TreZ route and the standalone TreS route are alternative module implementations, not a three-step chain. The narrower reusable TreY-TreZ route is also represented in modules/trey_trez_trehalose_biosynthesis.yaml; this broader module adds the alternative standalone TreS architecture. The PP_2918/Q88IT1 reaction is reversible, and its physiological direction in native KT2440 remains unresolved; inclusion here records demonstrated maltose-to-trehalose catalytic capacity, not established in vivo flux. PSEPK TreSB/Q88FN0 also carries a reversible TreS domain, but its fusion to maltokinase and its placement beside glgE support its separate treatment in the TreS-Mak-GlgE alpha-glucan-biosynthesis module. Five fresh OpenScientist jobs (three genes, generic module, and module + ppu00500 + PSEPK) finished without producing reports; no provider output was reconstructed or inferred.

5Nodes
2Parts
1Variant Sets
2Variants
3Annotons
1Connections

Derived QC

Recommended-field compliance

100.0% recommended fields populated

All recommended fields populated.

Module deep research

✗ none found

No MODULE:bacterial_trehalose_synthesis_from_alpha_glucans deep-research report alongside the module YAML.

Leaf nodes lacking representative members

✓ every leaf node grounds to a representative protein.

Template conformance

✓ every declared conforms_to bundle matches its template motif.

Gene-review completeness (3/6 grounded genes reviewed)

3 complete review(s) · 0 with deep research · 3 missing review · 3 reviewed but lacking deep research

Gene Review Complete Deep research
TreY (Arthrobacter sp. Q36) Q44315 ✗ — —
TreZ (Arthrobacter sp. Q36) Q44316 ✗ — —
TreS (Pseudomonas stutzeri CJ38) Q9LAS5 ✗ — —
treSA Q88IT1 ✓ ✓ ✗
treY Q88FN6 ✓ ✓ ✗
treZ Q88FN8 ✓ ✓ ✗

Details

Context
bacteriaNCBITaxon:2
Bacterial trehalose synthesis from alpha-glucans and maltoseMetabolic Pathwaybacterial_trehalose_synthesis_from_alpha_glucans
trehalose biosynthetic processGO:0005992
Context
bacteriaNCBITaxon:2
Variant set: Alpha-glucoside-dependent trehalose-synthesis route by substrate and enzyme architecture (One Or More)
Coupled TreY-TreZ route from alpha-1,4-glucanMetabolic Pathwaytrey_trez_route

TreY creates a trehalose-containing reducing end and TreZ releases free trehalose in a second reaction.

Connections

TreY supplies maltooligosyltrehalose to TreZ.
Part 1: maltooligosyltrehalose formation
TreY terminal glucosyl rearrangementReactiontrey_maltooligosyl_trehalose_formation

Annotons

Maltooligosyl trehalose synthase activity
trey_activity
Participant: Family: TreY maltooligosyl trehalose synthase family
Family:
TreY maltooligosyl trehalose synthase familyPANTHER:PTHR10357:SF216
Representative Members: TreY (Pseudomonas putida KT2440)UniProtKB:Q88FN6 TreY (Arthrobacter sp. Q36)UniProtKB:Q44315

Function

(1,4)-alpha-D-glucan 1-alpha-D-glucosylmutase activityGO:0047470
Substrates: alpha-1,4-glucan with a reducing-end alpha-1,4 linkage
Products: maltooligosyltrehalose

Rearranges the reducing-end glycosidic linkage to form the substrate consumed by TreZ.

Part 2: trehalose release
TreZ maltooligosyltrehalose hydrolysisReactiontrez_trehalose_release

Annotons

Maltooligosyltrehalose trehalohydrolase activity
trez_activity
Participant: Family: TreZ maltooligosyltrehalose trehalohydrolase family
Family:
TreZ maltooligosyltrehalose trehalohydrolase familyPANTHER:PTHR43651:SF11
Representative Members: TreZ (Pseudomonas putida KT2440)UniProtKB:Q88FN8 TreZ (Arthrobacter sp. Q36)UniProtKB:Q44316

Function

4-alpha-D-(1->4)-alpha-D-glucanotrehalose trehalohydrolase activityGO:0033942
Substrates: maltooligosyltrehalose water
Products: trehalose shortened alpha-1,4-glucan

Hydrolyzes the linkage adjacent to the trehalose moiety and releases free trehalose.

Standalone TreS route from maltoseReactionstandalone_tres_route

A standalone TreS reversibly interconverts maltose and trehalose; this route variant represents flux in the trehalose-forming direction.

Annotons

Maltose alpha-D-glucosyltransferase activity
tres_activity
Participant: Family: standalone TreS trehalose synthase family
Family:
standalone TreS trehalose synthase familyInterPro:IPR012665
Representative Members: TreSA (Pseudomonas putida KT2440)UniProtKB:Q88IT1 TreS (Pseudomonas stutzeri CJ38)UniProtKB:Q9LAS5

Function

maltose alpha-D-glucosyltransferase activityGO:0047471
Substrates: D-maltose
Products: alpha,alpha-trehalose

Carries the reversible reaction in the trehalose-forming direction without requiring the TreY-TreZ intermediate. For KT2440 PP_2918 this direction is demonstrated in vitro, while its physiological flux direction remains unresolved.