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3 hydroxy 3 methylglutaryl coa reductase encoding gene schmg1  (Azenta)

 
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    Structured Review

    Azenta 3 hydroxy 3 methylglutaryl coa reductase encoding gene schmg1
    Schematic of constructing engineered Y. lipolytica strain for squalene production. I indicate lipid droplet engineering to modulate triacylglycerols synthesis and increase squalene storage capacity. II indicates modulation of the MVA pathway to promote squalene synthesis flux. III indicates enzyme fusion engineering to promote catalytic efficiency between ERG20 and SQS. IV indicates iterative copy numbering of the <t>ScHMG1</t> gene. V indicates adaptive evolutionary engineering strategies. Red font represents endogenous genes, and blue font represents heterologous genes. DGA1, Diacylglycerol acyltransferase; LRO1, Phospholipid: diacylglycerol acyltransferase; ERG10, Acetyl-CoA acetyltransferase; ERG13, HMG-CoA synthase; ScHMG1, 3-hydroxy-3-methyl glutaryl coenzyme A reductase of S. cerevisiae origin; ERG20, farnesyl diphosphate synthase; SQS, squalene synthase.
    3 Hydroxy 3 Methylglutaryl Coa Reductase Encoding Gene Schmg1, supplied by Azenta, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/encode/3+3+coa+encoding+gene+hydroxy+methylglutaryl+reductase+schmg1/pmc12874323-53-1-16
    Average 86 stars, based on 1 article reviews
    3 hydroxy 3 methylglutaryl coa reductase encoding gene schmg1 - by Bioz Stars, 2026-10
    86/100 stars

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    1) Product Images from "Metabolic engineering and adaptive laboratory evolution enhance squalene production in Yarrowia lipolytica"

    Article Title: Metabolic engineering and adaptive laboratory evolution enhance squalene production in Yarrowia lipolytica

    Journal: Synthetic and Systems Biotechnology

    doi: 10.1016/j.synbio.2026.01.017

    Schematic of constructing engineered Y. lipolytica strain for squalene production. I indicate lipid droplet engineering to modulate triacylglycerols synthesis and increase squalene storage capacity. II indicates modulation of the MVA pathway to promote squalene synthesis flux. III indicates enzyme fusion engineering to promote catalytic efficiency between ERG20 and SQS. IV indicates iterative copy numbering of the ScHMG1 gene. V indicates adaptive evolutionary engineering strategies. Red font represents endogenous genes, and blue font represents heterologous genes. DGA1, Diacylglycerol acyltransferase; LRO1, Phospholipid: diacylglycerol acyltransferase; ERG10, Acetyl-CoA acetyltransferase; ERG13, HMG-CoA synthase; ScHMG1, 3-hydroxy-3-methyl glutaryl coenzyme A reductase of S. cerevisiae origin; ERG20, farnesyl diphosphate synthase; SQS, squalene synthase.
    Figure Legend Snippet: Schematic of constructing engineered Y. lipolytica strain for squalene production. I indicate lipid droplet engineering to modulate triacylglycerols synthesis and increase squalene storage capacity. II indicates modulation of the MVA pathway to promote squalene synthesis flux. III indicates enzyme fusion engineering to promote catalytic efficiency between ERG20 and SQS. IV indicates iterative copy numbering of the ScHMG1 gene. V indicates adaptive evolutionary engineering strategies. Red font represents endogenous genes, and blue font represents heterologous genes. DGA1, Diacylglycerol acyltransferase; LRO1, Phospholipid: diacylglycerol acyltransferase; ERG10, Acetyl-CoA acetyltransferase; ERG13, HMG-CoA synthase; ScHMG1, 3-hydroxy-3-methyl glutaryl coenzyme A reductase of S. cerevisiae origin; ERG20, farnesyl diphosphate synthase; SQS, squalene synthase.

    Techniques Used:

    Enhancing the expression of ScHMG1 to boost squalene synthesis . (A) Schematic design of overexpressing ScHMG1 at the IntC locus. (B) Effects of enhanced ScHMG1 expression on squalene and lipid synthesis in the engineered Y. lipolytica strain. (C) The pH, biomass, and glucose consumption of the engineered strains after 72 h of fermentation.
    Figure Legend Snippet: Enhancing the expression of ScHMG1 to boost squalene synthesis . (A) Schematic design of overexpressing ScHMG1 at the IntC locus. (B) Effects of enhanced ScHMG1 expression on squalene and lipid synthesis in the engineered Y. lipolytica strain. (C) The pH, biomass, and glucose consumption of the engineered strains after 72 h of fermentation.

    Techniques Used: Expressing

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    Article Title: Metabolic engineering and adaptive laboratory evolution enhance squalene production in Yarrowia lipolytica
    Article Snippet: .. The 3-hydroxy-3-methylglutaryl-CoA reductase encoding gene ScHMG1 (GenBank ID: 854900) from S. cerevisiae was codon-optimized and synthesized (Genewiz, Suzhou, China). .. Plasmid pUC19 was utilized for plasmid construction, and the recombinant plasmids were assembled in E. coli DH5α using the Clone Xpress II One Step Cloning Kit (Vazyme, Nanjing, China).

    Clone Assay:

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    Transformation Assay:

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    Plasmid Preparation:

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    Expressing:

    Article Title: A sulfotransferase from a gut microbe acts on diverse phenolic sulfate compounds, including acetaminophen sulfate
    Article Snippet: .. The gene encoding BvASST (gene ID 640760705; locus tag BVU_RS02960, formerly BVU_0583) was synthesized and codon-optimized for E. coli expression (Azenta Biosciences). ..

    Article Title: Structural basis for spectral red shift and UVA absorption in the microalgal water-soluble astaxanthin-binding protein AstaP-pink1.
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    Sequencing:

    Article Title: Structural basis for spectral red shift and UVA absorption in the microalgal water-soluble astaxanthin-binding protein AstaP-pink1.
    Article Snippet: AstaPs are water-soluble, photooxidative stress-inducible astaxanthin (AXT)-binding proteins found only in Scenedesmaceae microalgae, where they play a central role in survival under severe photooxidative stress.. Here, we focused on the unique function of AstaP-pink1, which converts orange AXT into a pink form and generates a UVA absorption spectrum upon protein binding.. AstaP-pink1 was expressed in genetically engineered Escherichia coli strains capable of synthesizing AXT.



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