SDSL Human

Serine Dehydratase-Like Human Recombinant
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Cat. No.
BT5406
Source
E.coli.
Synonyms
Serine dehydratase-like, SDS-RS1, Serine dehydratase 2, TDH, L-serine dehydratase/L-threonine deaminase, SDH 2, serine dehydratase related sequence 1, EC 4.3.1.17, EC 4.3.1.19.
Appearance
Sterile Filtered colorless solution.
Purity
Greater than 90% as determined by SDS-PAGE.
Usage
THE BioTek's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Description

Introduction to SDSL Human

SDSL Human, or Serine Dehydratase-Like, is a recombinant protein encoded by the SDSL gene (UniProt ID: Q96GA7). It belongs to the serine/threonine dehydratase family and functions as a pyridoxal phosphate (PLP)-dependent enzyme involved in glycine and serine metabolism . This protein is produced recombinantly in Escherichia coli and is widely used in biochemical and biomedical research due to its enzymatic activity and structural stability .

Formulation and Stability

  • Buffer: 20 mM Tris-HCl (pH 8.0), 2 mM DTT, 0.1 M NaCl, and 10% glycerol .

  • Storage:

    • Short-term: 4°C (2–4 weeks).

    • Long-term: -20°C with carrier protein (0.1% HSA/BSA) .

Enzymatic Activity

  • Primary Role: Catalyzes the dehydration of L-serine and L-threonine, producing pyruvate and α-ketobutyrate, respectively .

  • Cofactor: Requires pyridoxal phosphate (PLP) for activity .

  • Substrate Specificity: Higher activity toward serine compared to threonine .

Pathway Involvement

PathwayRole of SDSLAssociated Proteins
Glycine/Serine MetabolismSerine degradationSHMT1, ALDH7A1, GCSHA
Amino Acid BiosynthesisRegulation of serine levelsSDS, SRR

Therapeutic Targets

  • Cancer Biology: Mutations in SDSL’s PLP-binding domain (PDB ID: 2RKB) are linked to altered metabolic pathways in hepatic cancers .

  • Neurological Disorders: Potential role in oxidative stress mitigation via glycine-serine equilibrium .

Disease Associations

  • Thyroid Dyshormonogenesis: Linked to mutations affecting PLP-dependent enzymatic activity .

  • Metabolic Disorders: Altered SDSL expression correlates with impaired serine degradation .

Genetic Interactions

  • TUBGCP4: Direct interaction implicated in mitotic spindle regulation .

Future Directions

  • Therapeutic Development: Further exploration of SDSL inhibitors/activators for metabolic and oncological applications .

  • Structural Studies: High-resolution cryo-EM analysis to map conformational dynamics .

Product Specs

Introduction
Serine dehydratase L-serine ammonia-lyase (SDSL) is a member of the serine/threonine dehydratase family and acts as a serine-specific dehydratase. This enzyme utilizes pyridoxal phosphate as a cofactor and plays a crucial role in the metabolism of glycine and serine alongside two other key enzymes.
Description
Recombinant human SDSL, expressed in E. coli, is a single, non-glycosylated polypeptide chain comprising 353 amino acids (residues 1-329) with a molecular weight of 37.3 kDa. This protein is engineered with a 20 amino acid His-tag at the N-terminus and purified using proprietary chromatographic techniques.
Physical Appearance
Clear, colorless solution, sterile-filtered.
Formulation
The SDSL solution is supplied at a concentration of 0.5 mg/ml in a buffer consisting of 20mM Tris-HCl (pH 8.0), 2mM DTT, 0.1M NaCl, and 10% glycerol.
Stability
For short-term storage (2-4 weeks), the product can be stored at 4°C. For extended storage, freeze the solution at -20°C. The addition of a carrier protein (0.1% HSA or BSA) is recommended for long-term storage. Avoid repeated freeze-thaw cycles.
Purity
Purity is determined to be greater than 90% by SDS-PAGE analysis.
Synonyms
Serine dehydratase-like, SDS-RS1, Serine dehydratase 2, TDH, L-serine dehydratase/L-threonine deaminase, SDH 2, serine dehydratase related sequence 1, EC 4.3.1.17, EC 4.3.1.19.
Source
E.coli.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSHMDGPVA EHAKQEPFHV VTPLLESWAL SQVAGMPVFL KCENVQPSGS FKIRGIGHFC QEMAKKGCRH LVCSSGGNAG IAAAYAARKL GIPATIVLPE STSLQVVQRL QGEGAEVQLT GKVWDEANLR AQELAKRDGW ENVPPFDHPL IWKGHASLVQ ELKAVLRTPP GALVLAVGGG GLLAGVVAGL LEVGWQHVPI IAMETHGAHC FNAAITAGKL VTLPDITSVA KSLGAKTVAA RALECMQVCK IHSEVVEDTE AVSAVQQLLD DERMLVEPAC GAALAAIYSG LLRRLQAEGC LPPSLTSVVV IVCGGNNINS RELQALKTHL GQV.

Product Science Overview

Gene and Protein Structure

The SDSL gene is located on chromosome 12q24.13 and encodes a protein consisting of 329 amino acids with a molecular mass of approximately 34.7 kDa . The protein shares a significant sequence homology with hepatic serine dehydratase (SDH), indicating a conserved evolutionary pathway .

Enzymatic Activity

SDSL exhibits low serine dehydratase and threonine dehydratase activity. It also possesses glutamate racemase activity, which is crucial for the synthesis of D-glutamate and the degradation of L-serine and L-threonine . The enzyme’s activity is dependent on pyridoxal phosphate (PLP) as a cofactor but does not require metal ions or nucleotides .

Functional Significance

The enzyme plays a vital role in maintaining amino acid homeostasis within cells. It is involved in the isoleucine biosynthetic process and the threonine catabolic process . The dehydratase activity of SDSL contributes to the degradation of L-serine and L-threonine, while its racemase activity aids in the synthesis of D-glutamate .

Clinical Relevance

Mutations or dysregulation of the SDSL gene have been associated with certain diseases, including Spinocerebellar Ataxia, Autosomal Recessive 27, and Geographic Tongue . Understanding the function and regulation of SDSL can provide insights into these conditions and potential therapeutic targets.

Research and Applications

Recombinant human SDSL is used in various research applications to study its enzymatic properties and potential therapeutic uses. The recombinant protein is typically expressed in E. coli and purified for biochemical analyses .

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