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GoPubMed Proteins lists recent and important papers and reviews for proteins. Page last changed on 19 Dec 2016.

Lactate dehydrogenase A-like 6B

LDHL, lactate dehydrogenase A-like
Top mentioned proteins: ACID, HAD, CAN, OUT, V1a
Papers on LDHL
Reduction of d-lactate content in sauerkraut using starter cultures of recombinant Leuconostoc mesenteroides expressing the ldhL gene.
Han et al., Yanji, China. In J Biosci Bioeng, Nov 2015
To shift the metabolic flux of d-lactate from pyruvate to l-lactate, we expressed the l-lactate dehydrogenase (ldhL) gene in Leuconostoc mesenteroides ATCC 8293.
Regulation of metabolic flux in Lactobacillus casei for lactic acid production by overexpressed ldhL gene with two-stage oxygen supply strategy.
Zhang et al., Wuxi, China. In J Microbiol Biotechnol, 2015
The ldhL gene encoding L-lactate dehydrogenase (L-LDH) was overexpressed in L. casei, and a two-stage oxygen supply strategy (TOS) that maintained a medium oxygen supply level during the early fermentation phase, and a low oxygen supply level in the later phase was carried out.
Establishment of markerless gene deletion tools in thermophilic Bacillus smithii and construction of multiple mutant strains.
van Kranenburg et al., Wageningen, Netherlands. In Microb Cell Fact, 2014
RESULTS: Clean deletions of the ldhL gene were made in two B. smithii strains (DSM 4216(T) and compost isolate ET 138) by homologous recombination.
Major Role of NAD-Dependent Lactate Dehydrogenases in the Production of l-Lactic Acid with High Optical Purity by the Thermophile Bacillus coagulans.
Yu et al., Beijing, China. In Appl Environ Microbiol, 2014
Three enzymes responsible for lactic acid production-NAD-dependent l-lactate dehydrogenase (l-nLDH; encoded by ldhL), NAD-dependent d-lactate dehydrogenase (d-nLDH; encoded by ldhD), and glycolate oxidase (GOX)-were systematically investigated in order to study the relationship between these enzymes and the optical purity of lactic acid.
Kinetic characterization of recombinant Bacillus coagulans FDP-activated l-lactate dehydrogenase expressed in Escherichia coli and its substrate specificity.
Ouyang et al., Nanjing, China. In Protein Expr Purif, 2014
In this study, the gene ldhL encoding a thermostable l-LDH was amplified from B. coagulans NL01 genomic DNA and successfully expressed in Escherichia coli BL21 (DE3).
L-lactic acid production from D-xylose with Candida sonorensis expressing a heterologous lactate dehydrogenase encoding gene.
Penttilä et al., Espoo, Finland. In Microb Cell Fact, 2013
RESULTS: The yeast Candida sonorensis, which naturally metabolises D-xylose, was genetically modified to produce L-lactic acid from D-xylose by integrating the gene encoding L-lactic acid dehydrogenase (ldhL) from Lactobacillus helveticus into its genome.
Engineering and adaptive evolution of Escherichia coli W for L-lactic acid fermentation from molasses and corn steep liquor without additional nutrients.
Zhou et al., Wuhan, China. In Bioresour Technol, 2013
The D-lactic acid producing strain, Escherichia coli HBUT-D, was reengineered for L(+)-lactic acid fermentation by replacing the D-lactate dehydrogenase gene (ldhA) with an L(+)-lactate dehydrogenase gene (ldhL) from Pedicoccus acidilactici, followed by adaptive evolution in sucrose.
[Production of L-lactic acid from pentose by a genetically engineered Escherichia coli].
Wang et al., Wuhan, China. In Wei Sheng Wu Xue Bao, 2013
Then we cloned the L-lactate dehydrogenase gene (ldhL) of Pediococcus acidilactici and inserted it into the chromosome of JH01 via electroporation to obtain a recombinant strain Escherichia coli JH12.
Utilization of lactic acid bacterial genes in Synechocystis sp. PCC 6803 in the production of lactic acid.
Kondo et al., Kōbe, Japan. In Biosci Biotechnol Biochem, 2012
PCC 6803 to produce lactic acid using a lactate dehydrogenase (ldh) gene from various lactic acid-producing bacteria, Lactococcus lactis (ldhB and ldhX), Lactobacillus plantarum (ldhL and ldh), and Lactobacillus rhamnosus (ldhL).
Distribution dynamics of recombinant Lactobacillus in the gastrointestinal tract of neonatal rats.
Lin et al., Netherlands Antilles. In Plos One, 2012
We found that a combination of an L-lactate dehydrogenase (ldhL) promoter of Lactobacillus sakei with a backbone from pLEM415 yielded the highest level of reporter expression.
Homofermentative production of optically pure L-lactic acid from xylose by genetically engineered Escherichia coli B.
Zhou et al., Wuhan, China. In Microb Cell Fact, 2012
RESULTS: In this study, an ethanologenic Escherichia coli strain, SZ470 (ΔfrdBC ΔldhA ΔackA ΔpflB ΔpdhR ::pflBp6-acEF-lpd ΔmgsA), was reengineered for homofermentative production of L-lactic acid from xylose (1.2 mole xylose = > 2 mole L-lactic acid), by deleting the alcohol dehydrogenase gene (adhE) and integrating the L-lactate dehydrogenase gene (ldhL) of Pediococcus acidilactici.
Transformation of, and heterologous protein expression in, Lactobacillus agilis and Lactobacillus vaginalis isolates from the chicken gastrointestinal tract.
Allison et al., Canberra, Australia. In Appl Environ Microbiol, 2011
Transformants of both La3 and Lv5 containing the La3 ldhL promoter were the most fluorescent.
Changes in tear protein profile in patients with conjunctivochalasis.
Durán et al., Spain. In Cornea, 2011
Eleven protein spots were identified, which included proteins belonging to the S100 family (A8, A9, A4; 2.44, 1.71, and 2.82 fold upregulation, respectively), guanosine triphosphate-binding protein 2 (1.95 fold), l-lactate dehydrogenase A-like 6B (2.32 fold), fatty acid-binding protein (2.01 fold), keratin type I cytoskeletal 10 (1.81 fold), glutathione S-transferase P (2.27 fold), peroxiredoxin-1, peroxiredoxin-5 (1.79- and 1.92 fold, respectively), and cullin-4B+ glyceraldehyde 3-phosphate dehydrogenase (1.96 fold).
Comparison of expression vectors in Lactobacillus reuteri strains.
Lucchini et al., Cremona, Italy. In Fems Microbiol Lett, 2010
The promoters of the Lactobacillus acidophilus surface layer protein gene (slp), L. acidophilus lactate dehydrogenase gene (ldhL) and enterococcal rRNA adenine N-6-methyltransferase gene (ermB) were fused to the coding sequence of EGFP and inserted into the backbone of the pTRKH3 shuttle vector (pTRKH3-slpGFP, pTRKH3-ldhGFP, pTRKH3-ermGFP).
Molecular genetic characterization of the thermostable L-lactate dehydrogenase gene (ldhL) of Thermoanaerobacter ethanolicus JW200 and biochemical characterization of the enzyme.
Shao et al., Nanjing, China. In Biochemistry (mosc), 2010
The structural gene ldhL for a thermostable L-(+)-lactate dehydrogenase was cloned from Thermoanaerobacter ethanolicus JW200.
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