Recombinant Photobacterium profundum Bifunctional protein GlmU (glmU)

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Cat. No.
BT1162353
Source
Yeast
Synonyms
glmU; PBPRA3601Bifunctional protein GlmU [Includes: UDP-N-acetylglucosamine pyrophosphorylase; EC 2.7.7.23; N-acetylglucosamine-1-phosphate uridyltransferase); Glucosamine-1-phosphate N-acetyltransferase; EC 2.3.1.157)]
Purity
>85% (SDS-PAGE)
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Cat. No.
BT1162353
Source
E.coli
Synonyms
glmU; PBPRA3601Bifunctional protein GlmU [Includes: UDP-N-acetylglucosamine pyrophosphorylase; EC 2.7.7.23; N-acetylglucosamine-1-phosphate uridyltransferase); Glucosamine-1-phosphate N-acetyltransferase; EC 2.3.1.157)]
Purity
>85% (SDS-PAGE)
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Cat. No.
BT1162353
Source
E.coli
Synonyms
glmU; PBPRA3601Bifunctional protein GlmU [Includes: UDP-N-acetylglucosamine pyrophosphorylase; EC 2.7.7.23; N-acetylglucosamine-1-phosphate uridyltransferase); Glucosamine-1-phosphate N-acetyltransferase; EC 2.3.1.157)]
Purity
>85% (SDS-PAGE)
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Cat. No.
BT1162353
Source
Baculovirus
Synonyms
glmU; PBPRA3601Bifunctional protein GlmU [Includes: UDP-N-acetylglucosamine pyrophosphorylase; EC 2.7.7.23; N-acetylglucosamine-1-phosphate uridyltransferase); Glucosamine-1-phosphate N-acetyltransferase; EC 2.3.1.157)]
Purity
>85% (SDS-PAGE)
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Cat. No.
BT1162353
Source
Mammalian cell
Synonyms
glmU; PBPRA3601Bifunctional protein GlmU [Includes: UDP-N-acetylglucosamine pyrophosphorylase; EC 2.7.7.23; N-acetylglucosamine-1-phosphate uridyltransferase); Glucosamine-1-phosphate N-acetyltransferase; EC 2.3.1.157)]
Purity
>85% (SDS-PAGE)
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Description

Functional Domains and Mechanism

GlmU is a bifunctional enzyme with two distinct active sites:

  • C-terminal acetyltransferase domain: Transfers an acetyl group from acetyl-CoA to glucosamine-1-phosphate (GlcN-1-P), forming GlcNAc-1-P .

  • N-terminal uridyltransferase domain: Catalyzes the transfer of UMP from UTP to GlcNAc-1-P, generating UDP-GlcNAc .

Structural studies in related species (e.g., E. coli, Mycobacterium tuberculosis) reveal that GlmU forms a trimeric structure, with acetyltransferase active sites formed at the junction of adjacent subunits . The enzyme’s substrate specificity for UTP over ATP is critical for its role in cell wall biosynthesis .

Drug Discovery

GlmU is a validated antimicrobial target due to its essential role in bacterial viability and absence in humans . Inhibitors targeting its acetyltransferase domain (e.g., arylsulfonamides) or uridyltransferase domain (e.g., aminopiperidine derivatives) have shown promise in disrupting biofilm formation and bacterial growth .

Comparative Analysis with Other Bacterial GlmU

FeaturePhotobacterium profundum GlmUE. coli GlmUM. tuberculosis GlmU
Sequence ConservationHigh in acetyltransferase domain75% identity68% identity
EssentialityRequired for biofilm formationEssential for growth Drug target
Inhibitors TestedLimited dataThiol-reactive agents 2-phenylbenzofurans

Practical Considerations for Use

  • Reconstitution: Dissolve lyophilized protein in deionized water (0.1–1.0 mg/mL) with 50% glycerol for stability .

  • Activity Assays: Monitor UDP-GlcNAc production via HPLC or enzymatic coupled assays .

  • Crystallization: Requires substrate-bound conditions (e.g., GlcN-1-P and UTP) for active-site visualization .

Future Directions

Further studies could explore:

  • Photobacterium-specific inhibitors: Leverage structural differences from human homolog UAP1 for selective drug design .

  • Deep-sea adaptations: Investigate how high-pressure environments influence GlmU’s enzymatic efficiency .

Product Specs

Form
Lyophilized powder
Note: We will prioritize shipping the format currently in stock. However, if you require a specific format, please indicate your preference in the order notes. We will prepare the product according to your request.
Lead Time
Delivery time may vary based on the purchasing method or location. Please consult your local distributors for specific delivery time details.
Note: Our proteins are typically shipped with standard blue ice packs. If dry ice shipping is required, please contact us in advance as additional fees will apply.
Notes
Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.
Reconstitution
We recommend centrifuging the vial briefly before opening to collect the contents at the bottom. Reconstitute the protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL. We suggest adding 5-50% glycerol (final concentration) and aliquoting for long-term storage at -20°C/-80°C. Our standard glycerol final concentration is 50%. Customers can use this as a reference.
Shelf Life
The shelf life is influenced by various factors including storage conditions, buffer composition, temperature, and the intrinsic stability of the protein itself.
Generally, liquid forms have a shelf life of 6 months at -20°C/-80°C. Lyophilized forms have a shelf life of 12 months at -20°C/-80°C.
Storage Condition
Store at -20°C/-80°C upon receipt. Aliquoting is necessary for multiple uses. Avoid repeated freeze-thaw cycles.
Tag Info
Tag type will be determined during the manufacturing process.
The specific tag type will be determined during production. If you have a preference for a specific tag, please inform us, and we will prioritize its inclusion in the development process.
Synonyms
glmU; PBPRA3601Bifunctional protein GlmU [Includes: UDP-N-acetylglucosamine pyrophosphorylase; EC 2.7.7.23; N-acetylglucosamine-1-phosphate uridyltransferase); Glucosamine-1-phosphate N-acetyltransferase; EC 2.3.1.157)]
Buffer Before Lyophilization
Tris/PBS-based buffer, 6% Trehalose.
Datasheet
Please contact us to get it.
Expression Region
1-453
Protein Length
full length protein
Purity
>85% (SDS-PAGE)
Species
Photobacterium profundum (strain SS9)
Target Names
glmU
Target Protein Sequence
MSFSAVILAA GKGTRMYSNV PKVLHTLAGK PMAKHVIDTC SDLGASHIHL VYGHGGDTMQ QVLADEPVSW ILQAEQLGTG HAVNQASSGL ADNEKVLILY GDVPLISGDT LTNLLDAQPD GGIALLTVVL DNPVGYGRIV RRNGPVVAIV EQKDASEEQK LIKEINTGVM VANGGDLKRW LGQLKNENSQ GEYYLTDIIA IAHDEGRAVE AVHPVNPIEV EGVNNRIQLA RLERAYQAMQ AERLLEQGVM LRDPSRFDLR GKLQCGTDVE IDVNVIIEGN VSIGNNVLIG TGCVLKDCEI DDNSVIRPYS VIEGATVGED CTVGPFTRLR PGAELVGDSH VGNFVEMKKS RLGRGSKANH LTYLGDADIG DRVNIGAGTI TCNYDGVNKF KTEIGDDVFV GSDTQLIAPV KIGKGATIGA GATINRDIGE GELVITRAPA RTIKGWKRPV KQK
Uniprot No.
Q6LLH1

Target Background

Function
This bifunctional protein catalyzes the final two sequential reactions in the de novo biosynthetic pathway for UDP-N-acetylglucosamine (UDP-GlcNAc). The C-terminal domain facilitates the transfer of an acetyl group from acetyl coenzyme A to glucosamine-1-phosphate (GlcN-1-P), resulting in the production of N-acetylglucosamine-1-phosphate (GlcNAc-1-P). Subsequently, the N-terminal domain catalyzes the transfer of uridine 5-monophosphate (from uridine 5-triphosphate) to GlcNAc-1-P, generating UDP-GlcNAc.
Database Links

KEGG: ppr:PBPRA3601

STRING: 298386.PBPRA3601

Protein Families
N-acetylglucosamine-1-phosphate uridyltransferase family; Transferase hexapeptide repeat family
Subcellular Location
Cytoplasm.

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