Recombinant Bacillus amyloliquefaciens Serine hydroxymethyltransferase (glyA)

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Cat. No.
BT55402
Source
Yeast
Synonyms
glyA; RBAM_034060; Serine hydroxymethyltransferase; SHMT; Serine methylase; EC 2.1.2.1
Purity
>85% (SDS-PAGE)
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Cat. No.
BT55402
Source
E.coli
Synonyms
glyA; RBAM_034060; Serine hydroxymethyltransferase; SHMT; Serine methylase; EC 2.1.2.1
Purity
>85% (SDS-PAGE)
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Cat. No.
BT55402
Source
E.coli
Synonyms
glyA; RBAM_034060; Serine hydroxymethyltransferase; SHMT; Serine methylase; EC 2.1.2.1
Purity
>85% (SDS-PAGE)
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Cat. No.
BT55402
Source
Baculovirus
Synonyms
glyA; RBAM_034060; Serine hydroxymethyltransferase; SHMT; Serine methylase; EC 2.1.2.1
Purity
>85% (SDS-PAGE)
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Cat. No.
BT55402
Source
Mammalian cell
Synonyms
glyA; RBAM_034060; Serine hydroxymethyltransferase; SHMT; Serine methylase; EC 2.1.2.1
Purity
>85% (SDS-PAGE)
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Description

Molecular Characterization

Recombinant GlyA from B. amyloliquefaciens is engineered with a His tag for purification, expressed in Saccharomyces cerevisiae or Escherichia coli systems . Key features include:

PropertyDetails
Host SystemYeast (S. cerevisiae) or E. coli
Amino Acid RangeAA 1–415
TagN-terminal His tag
Purity>90% (confirmed via SDS-PAGE)
StorageLyophilized in PBS (pH 7.4) with 50% glycerol; stable at -20°C

The glyA gene (UniProt ID: A0RLA3) encodes a 415-residue protein conserved across Bacillus species, with high sequence similarity to homologs in B. subtilis and B. stearothermophilus .

Functional Roles in Metabolism

GlyA is essential for:

  1. Folate Metabolism: Supplies one-carbon units for nucleotide and methionine biosynthesis .

  2. Amino Acid Homeostasis: Balances serine/glycine pools and contributes to D-alanine synthesis in species lacking dedicated alanine racemases .

  3. Stress Adaptation: Linked to biofilm regulation via modulation of S-adenosylmethionine (SAM) and cyclic-di-GMP levels in related Bacillus species .

Industrial and Biotechnological Applications

  • Metabolic Engineering: CRISPR/Cas9n systems enable efficient glyA knockout or overexpression in B. amyloliquefaciens to optimize secondary metabolite production .

  • Enzyme Production: Recombinant GlyA is utilized in high-throughput assays for folate pathway analysis and inhibitor screening .

Key Research Findings

  • Substrate Specificity: GlyA from B. amyloliquefaciens exhibits broad specificity, catalyzing serine/glycine interconversion, alanine racemization, and threonine cleavage .

  • Inhibitor Sensitivity: Activity is suppressed by D-cycloserine, a D-Ala analog, highlighting its role in peptidoglycan precursor synthesis .

  • Thermostability: Retains >80% activity after 1 hour at 50°C, suitable for industrial processes .

Challenges and Future Directions

While recombinant GlyA is robustly produced, optimizing its catalytic efficiency for non-natural substrates (e.g., D-serine) remains a focus. Advances in B. amyloliquefaciens genetic toolkits, such as bicistronic vectors and promoter engineering, are expected to enhance yields and application scope .

Product Specs

Form
Lyophilized powder. We will preferentially ship the format we have in stock. If you have special format requirements, please note them when ordering, and we will fulfill your request.
Lead Time
Delivery times vary depending on the purchase method and location. Consult your local distributor for specific delivery times. All proteins are shipped with standard blue ice packs. For dry ice shipping, please contact us in advance; additional fees apply.
Notes
Avoid repeated freezing and thawing. Store working aliquots at 4°C for up to one week.
Reconstitution
Briefly centrifuge the vial before opening to collect contents at the bottom. Reconstitute the protein in sterile deionized water to 0.1-1.0 mg/mL. We recommend adding 5-50% glycerol (final concentration) and aliquoting for long-term storage at -20°C/-80°C. Our default final glycerol concentration is 50%.
Shelf Life
Shelf life depends on several factors: storage conditions, buffer components, storage temperature, and protein stability. Generally, the liquid form has a 6-month shelf life at -20°C/-80°C, while the lyophilized form has a 12-month shelf life at -20°C/-80°C.
Storage Condition
Store at -20°C/-80°C upon receipt. Aliquot for multiple uses. Avoid repeated freeze-thaw cycles.
Tag Info
The tag type will be determined during the manufacturing process. If you require a specific tag, please inform us, and we will prioritize its development.
Synonyms
glyA; RBAM_034060; Serine hydroxymethyltransferase; SHMT; Serine methylase; EC 2.1.2.1
Buffer Before Lyophilization
Tris/PBS-based buffer, 6% Trehalose.
Datasheet
Please contact us to get it.
Expression Region
1-415
Protein Length
full length protein
Purity
>85% (SDS-PAGE)
Species
Bacillus velezensis (strain DSM 23117 / BGSC 10A6 / FZB42) (Bacillus amyloliquefaciens subsp. plantarum)
Target Names
glyA
Target Protein Sequence
MKHLPVQDKQ VFNAIKDERK RQQTKIELIA SENFVTEAVM EAQGSVLTNK YAEGYPGKRY YGGCEHVDVV EDIARDRAKE IFGAEHVNVQ PHSGAQANMA VYFTILEHGD TVLGMNLSHG GHLTHGSPVN FSGVQYNFVE YGVDKDTQYI DYEDVREKAL AHKPKLIVAG ASAYPRTIDF KKFREIADEV GAYFMVDMAH IAGLVAAGLH PNPVPYADFV TTTTHKTLRG PRGGMILCRE EFGKKIDKSI FPGIQGGPLM HVIAAKAVSF GEVLEDDFKT YAQNVISNAK SLAESLNKEG IQLVSGGTDN HLVLVDLRSL GLTGKVAEHV LDEIGITSNK NAIPYDPEKP FVTSGIRLGT AAVTSRGFDG DALEEVGAII GLALKHHEDE AKLEEARQRV SALTEKFPLY KELGY
Uniprot No.
A7Z9Q9

Target Background

Function
Catalyzes the reversible interconversion of serine and glycine, using tetrahydrofolate (THF) as the one-carbon carrier. This reaction is the primary source of one-carbon units needed for biosynthesis of purines, thymidylate, methionine, and other essential biomolecules. Also exhibits THF-independent aldolase activity with beta-hydroxyamino acids, producing glycine and aldehydes through a retro-aldol mechanism.
Database Links

KEGG: bay:RBAM_034060

Protein Families
SHMT family
Subcellular Location
Cytoplasm.

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