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Molecular Genetics and Metabolism, ISSN 1096-7192, 09/2017, Volume 122, Issue 1-2, pp. 135 - 142
Journal Article
Molecular Systems Biology, ISSN 1744-4292, 11/2010, Volume 6, Issue 1, pp. 436 - n/a
Bacterial genomes encode hundreds to thousands of enzymes, most of which are specialized for particular functions. However, most enzymes have inefficient... 
multicopy suppression | metabolic bypass | promiscuity | pyridoxal‐5′‐phosphate | serendipitouspathway | serendipitous pathway | K-12 | D-3-PHOSPHOGLYCERATE DEHYDROGENASE | ALKALINE-PHOSPHATASE | BIOCHEMISTRY & MOLECULAR BIOLOGY | ESCHERICHIA-COLI | ENZYMATIC-ACTIVITIES | pyridoxal-5 '-phosphate | SUGAR KINASES | SYNTHASE | EVOLUTION | BIOSYNTHESIS | VITAMIN-B6 | Gene Expression Regulation, Enzymologic - drug effects | Escherichia coli - enzymology | Pyridoxal Phosphate - biosynthesis | Oxidoreductases - metabolism | Oxidoreductases - genetics | Serine - biosynthesis | Glucose - pharmacology | Escherichia coli Proteins - physiology | Gene Expression Regulation, Bacterial - drug effects | Metabolic Networks and Pathways - genetics | Genes, Bacterial - physiology | Epistasis, Genetic - physiology | Carbohydrate Dehydrogenases - physiology | Escherichia coli - genetics | Models, Biological | Escherichia coli - metabolism | Escherichia coli Proteins - genetics | Metabolic Networks and Pathways - physiology | Microbiological Techniques | Escherichia coli - growth & development | Organisms, Genetically Modified | Carbohydrate Dehydrogenases - genetics | Phosphates | Enzymes | Yeast | Dehydrogenases | Serine | Alcohol | Genomes | Biosynthesis | Glucose | Metabolism | Kinases | Gene expression | Patched protein | Serendipity | Pathways | E coli | Metabolites | Plasmids | Physiology | Metabolic pathways | Mutation
Journal Article
BBA - Proteins and Proteomics, ISSN 1570-9639, 09/2015, Volume 1854, Issue 9, pp. 1167 - 1174
Journal Article
Journal Article
Proteins: Structure, Function, and Bioinformatics, ISSN 0887-3585, 10/2014, Volume 82, Issue 10, pp. 2831 - 2841
ABSTRACT Serine hydroxymethyltransferase (SHMT) is a pyridoxal‐5′‐phosphate (PLP)‐dependent enzyme belonging to the fold type I superfamily, which catalyzes in... 
psychrophilic enzyme | flexibility | homology modeling | conformational transition | B' factors | pyridoxal‐5′‐phosphate | X‐ray crystallography | serine hydroxymethyltransferase | holo enzyme | apo enzyme | Apo enzyme | Pyridoxal-5′-phosphate | X-ray crystallography | Serine hydroxymethyltransferase | Holo enzyme | Homology modeling | Psychrophilic enzyme | Flexibility | Conformational transition | APO | MECHANISM | RECOGNITION | CRYSTAL-STRUCTURE | BIOCHEMISTRY & MOLECULAR BIOLOGY | ESCHERICHIA-COLI | COMPLEXES | pyridoxal-5 '-phosphate | MULTIPLE SEQUENCE ALIGNMENT | PYRIDOXAL 5'-PHOSPHATE | ENZYME | BIOPHYSICS | SECONDARY STRUCTURE | Pyridoxal Phosphate - chemistry | Salmonella typhimurium - growth & development | Bacterial Proteins - chemistry | Crystallography, X-Ray | Pyridoxal Phosphate - metabolism | Coenzymes - metabolism | Glycine Hydroxymethyltransferase - chemistry | Databases, Protein | Apoenzymes - metabolism | Escherichia coli - growth & development | Salmonella typhimurium - enzymology | Coenzymes - chemistry | Recombinant Proteins - metabolism | Glycine Hydroxymethyltransferase - genetics | Catalytic Domain | Gammaproteobacteria - enzymology | Escherichia coli - enzymology | Protein Structure, Secondary | Bacterial Proteins - genetics | Enzyme Stability | Models, Molecular | Recombinant Proteins - chemistry | Escherichia coli Proteins - metabolism | Mutant Proteins - metabolism | Gammaproteobacteria - growth & development | Glycine Hydroxymethyltransferase - metabolism | Protein Folding | Apoenzymes - genetics | Mutant Proteins - chemistry | Apoenzymes - chemistry | Escherichia coli Proteins - genetics | Protein Binding | Bacterial Proteins - metabolism | Protein Conformation | Escherichia coli Proteins - chemistry
Journal Article
The Journal of Nutrition, ISSN 0022-3166, 08/2019, Volume 149, Issue 8, pp. 1354 - 1362
ABSTRACT Background Vitamin B-6 (B-6), in the form of pyridoxal 5′phosphate (PLP), is critical for one-carbon metabolism reactions and cellular function.... 
HOMOCYSTEINE | functional indicator | VITAMIN-B-6 RESTRICTION | SERINE HYDROXYMETHYLTRANSFERASE | YOUNG MEN | B-VITAMIN | pregnancy | pyridoxal-5 '-phosphate | one-carbon metabolism | FOOD-FREQUENCY QUESTIONNAIRE | vitamin B-6 | NUTRITION & DIETETICS | AMINO-ACIDS | cystathionine | FOLATE | METHIONINE
Journal Article
International Journal of Biological Macromolecules, ISSN 0141-8130, 06/2019, Volume 131, pp. 912 - 924
Human pyridoxal 5′-phosphate phosphatase (PLPP), also known as a chronophin, is a phosphatase belonging to subfamily II of the HAD phosphatases, characterized... 
HAD phosphatase | Pyridoxal-5′-phosphate phosphatase | Chronophin | Phosphotransfer | Crystal structure | POLYMER SCIENCE | PROVIDE INSIGHT | MECHANISM | BIOCHEMISTRY & MOLECULAR BIOLOGY | COFILIN | REFINEMENT | ENZYMES | PURIFICATION | Pyridoxal-5 '-phosphate phosphatase | VITAMIN-B6 | CHEMISTRY, APPLIED | EXPRESSION | PHOSPHATASES | Phosphates | Enzymes | Phosphatases | Peptides | Analysis | Crystals | Structure
Journal Article
EMBO reports, ISSN 1469-221X, 09/2003, Volume 4, Issue 9, pp. 850 - 854
Journal Article
Journal Article
Journal of Bioscience and Bioengineering, ISSN 1389-1723, 11/2014, Volume 118, Issue 5, pp. 496 - 501
A novel enzyme, which catalyzed decarboxylation of -lysine into cadaverine with release of carbon dioxide and oxidative deamination of -lysine into... 
l-Amino acid oxidase | Pyridoxal-5′-phosphate | l-Lysine oxidase | l-Amino acid decarboxylase | Putrescine oxidase | l-Lysine decarboxylase | Burkholderia | l-Lysine | Pyridoxal-5'-phosphate | L-Lysine decarboxylase | L-Lysine oxidase | L-Lysine | L-Amino acid oxidase | L-Amino acid decarboxylase | EPSILON-OXIDASE | SPECIFICITY | FOOD SCIENCE & TECHNOLOGY | ESCHERICHIA-COLI | ORNITHINE-DECARBOXYLASE | ARGININE DECARBOXYLASE | ALPHA-OXIDASE | ENZYME | BIOTECHNOLOGY & APPLIED MICROBIOLOGY | PURIFICATION | Pyridoxal-5 '-phosphate | AMINO-ACID OXIDASE | NEUROSPORA-CRASSA | Amino Acid Sequence | Molecular Weight | Oxidation-Reduction | Molecular Sequence Data | Substrate Specificity | Carboxy-Lyases - chemistry | Amino Acid Oxidoreductases - metabolism | Pyridoxal Phosphate - metabolism | Carboxy-Lyases - biosynthesis | Coenzymes - metabolism | Carboxy-Lyases - isolation & purification | Burkholderia - enzymology | Escherichia coli - genetics | Decarboxylation | Isoelectric Point | Amino Acid Oxidoreductases - chemistry | Escherichia coli - metabolism | Protein Conformation | Amino Acid Oxidoreductases - isolation & purification | Carboxy-Lyases - metabolism | Lysine - metabolism | Amino Acid Oxidoreductases - biosynthesis | Oxidases | Phosphates | Ammonia | Hydrogen peroxide | Implants, Artificial | Prosthesis | Lysine | Chemical properties
Journal Article
Journal Article