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1. Orotidine monophosphate decarboxylase
: a mechanistic dialogue
by Lee, Jeehiun K and Tantillo, D. J and SpringerLink (Online service)
2004, Topics in current chemistry, ISBN 9783540205661, Volume 238., viii, 151
Enzymes | Catalysis | Decarboxylation | Analysis | Biochemistry, general | Theoretical and Computational Chemistry | Chemistry | Chemistry, Organic | Chemistry, Physical organic | Physical Chemistry | Characterization and Evaluation of Materials | Biochemistry | Enzymology | Surfaces (Physics) | Organic Chemistry
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2. Full Text The Enigmatic P450 Decarboxylase OleT Is Capable of, but Evolved to Frustrate, Oxygen Rebound Chemistry
by Hsieh, Chun H and Huang, Xiongyi and Amaya, José A and Rutland, Cooper D and Keys, Carson L and Groves, John T and Austin, Rachel N and Makris, Thomas M
Biochemistry, ISSN 0006-2960, 07/2017, Volume 56, Issue 26, pp. 3347 - 3357
OleT is a cytochrorrie P450 enzyme that catalyzes the removal of carbon dioxide from variable chain length fatty acids to form 1-alkenes. In this work, we... 
COMPOUND-I | DIIRON ALKANE MONOOXYGENASE | ALIPHATIC HYDROXYLATION | BIOCHEMISTRY & MOLECULAR BIOLOGY | CLOCK SUBSTRATE PROBES | CYTOCHROME-P450 PEROXYGENASE | FATTY-ACIDS | SOLUBLE METHANE MONOOXYGENASE | KINETIC CHARACTERIZATION | OLEOVORANS ALKB HYDROXYLATES | AROMATIC PEROXYGENASE | Guaiacol - metabolism | Molecular Conformation | Bacterial Proteins - chemistry | Cytochrome P-450 Enzyme System - metabolism | Substrate Specificity | Lauric Acids - metabolism | Caprylates - metabolism | Decanoic Acids - metabolism | Carboxy-Lyases - genetics | Cyclopropanes - chemistry | Hydrogen Peroxide - chemistry | Terpenes - chemistry | Lauric Acids - chemistry | Terpenes - metabolism | Decanoic Acids - chemistry | Carboxy-Lyases - metabolism | Caproates - metabolism | Micrococcus - enzymology | Catalytic Domain | Biocatalysis | Oxidation-Reduction | Bacterial Proteins - genetics | Cyclopropanes - metabolism | Models, Molecular | Carboxy-Lyases - chemistry | Caprylates - chemistry | Hydrogen Peroxide - metabolism | Cytochrome P-450 Enzyme System - chemistry | Decarboxylation | Biofuels - analysis | Cytochrome P-450 Enzyme System - genetics | Bacterial Proteins - metabolism | Chemical bonds | Hydrogen peroxide | Research | Liquid fuels | Analysis | Decarboxylases
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3. Full Text Chemical Profiling of the Endoplasmic Reticulum Proteome Using Designer Labeling Reagents
by Fujisawa, Alma and Tamura, Tomonori and Yasueda, Yuki and Kuwata, Keiko and Hamachi, Itaru
Journal of the American Chemical Society, ISSN 0002-7863, 12/2018, Volume 140, Issue 49, pp. 17060 - 17070
The endoplasmic reticulum (ER) is an organelle that performs a variety of essential cellular functions via interactions with other organelles. Despite its... 
PROTEINS | CHEMISTRY, MULTIDISCIPLINARY | STRESS-RESPONSE | LIVING CELLS | MOLECULES | Xanthenes - chemical synthesis | Multifunctional Enzymes - chemistry | Humans | Cyclophilin A - chemistry | Endoplasmic Reticulum - metabolism | Proteome - chemistry | Tandem Mass Spectrometry | Endoplasmic Reticulum - chemistry | Thioredoxins - analysis | Peptide Synthases - chemistry | Chromatography, Liquid | Proteomics - methods | Thioredoxins - chemistry | Unfolded Protein Response - drug effects | Endoplasmic Reticulum Stress - drug effects | Multifunctional Enzymes - analysis | Xanthenes - chemistry | Carboxy-Lyases - analysis | Carboxy-Lyases - chemistry | Molecular Probes - chemical synthesis | Proteome - analysis | Molecular Probes - chemistry | Cyclophilin A - analysis | Tunicamycin - pharmacology | Peptide Synthases - analysis | HeLa Cells
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4. Full Text Designer Micelles Accelerate Flux Through Engineered Metabolism in E. coli and Support Biocompatible Chemistry
by Wallace, Stephen and Balskus, Emily P
Angewandte Chemie International Edition, ISSN 1433-7851, 05/2016, Volume 55, Issue 20, pp. 6023 - 6027
Synthetic biology has enabled the production of many value‐added chemicals via microbial fermentation. However, the problem of low product titers from... 
synthetic biology | catalysis | metabolism | sustainable chemistry | micelles | ROOM-TEMPERATURE | BACTERIA | TOLERANCE | SOLVENT-IMPREGNATED RESINS | CHEMISTRY, MULTIDISCIPLINARY | AMPHIPHILE | SURFACTANT | CHEMICALS | MIYAURA CROSS-COUPLINGS | WATER | Metabolic Engineering | Green Chemistry Technology | Microscopy, Electron, Transmission | Arabidopsis - enzymology | Phenylalanine - metabolism | Styrene - metabolism | Biocompatible Materials - chemistry | Phenylalanine Ammonia-Lyase - metabolism | Arabidopsis Proteins - metabolism | Biocompatible Materials - chemical synthesis | Styrene - chemistry | Phenylalanine - chemistry | Micelles | Escherichia coli - metabolism | Saccharomyces cerevisiae - enzymology | Carboxy-Lyases - metabolism | Vitamin E - chemistry | Fungal Proteins - metabolism | Surface active agents | Transition metal compounds | Metal catalysts | Escherichia coli | Cyclopropane compounds | Green technology | Physiological aspects | Permeability | Catalysis | Fermentation | Metabolism | Biotechnology | Fluctuations | Catalysts | Membrane permeability | Flux | Surfactants | Sustainable yield | Renewable resources | Molecular chains | Organic chemistry | Metabolic flux | Chemistry | Microorganisms | E coli | Vitamin E | Styrene | Metabolic engineering | Biocompatibility | Tocopherol | Pollutants | Recombinant | Synthetic Biology | Sustainable Chemistry
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5. Full Text Mechanistic elucidation of the mycofactocin-biosynthetic radical S-adenosylmethionine protein, MftC
by Khaliullin, Bulat and Ayikpoe, Richard and Tuttle, Mason and Latham, John A
Journal of Biological Chemistry, ISSN 0021-9258, 2017, Volume 292, Issue 31, pp. 13022 - 13033
Ribosomally synthesized and posttranslationally modified peptide (RiPP) pathways produce a diverse array of natural products. A subset of these pathways... 
S-adenosylmethionine (SAM) | CROSS-LINK | peptide biosynthesis | radical | SAM ENZYME | BIOCHEMISTRY & MOLECULAR BIOLOGY | MftC | MATURATION | THIOETHER BOND FORMATION | PQQD | PEPTIDE CHAPERONE | mycofactocin | NMR-SPECTRA | CATALYZES | C-ALPHA | iron-sulfur protein | enzyme mechanism | POSTTRANSLATIONAL MODIFICATION | Molecular Chaperones - metabolism | Protein Precursors - chemistry | Stereoisomerism | Bacterial Proteins - chemistry | Chromatography, High Pressure Liquid | Molecular Chaperones - chemistry | Carboxy-Lyases - genetics | Recombinant Fusion Proteins - metabolism | Valine - chemistry | Tandem Mass Spectrometry | Tyramine - chemistry | Spectrometry, Mass, Electrospray Ionization | Nuclear Magnetic Resonance, Biomolecular | Carboxy-Lyases - metabolism | Protein Interaction Domains and Motifs | Mycobacterium ulcerans - enzymology | Tyramine - metabolism | Tyrosine - chemistry | Biocatalysis | Mutagenesis, Site-Directed | Protein Precursors - genetics | Oxidation-Reduction | Bacterial Proteins - genetics | Molecular Chaperones - genetics | Carboxy-Lyases - chemistry | Recombinant Fusion Proteins - chemistry | Protein Precursors - metabolism | Mycobacterium ulcerans - metabolism | Tyrosine - metabolism | Valine - metabolism | Decarboxylation | Bacterial Proteins - metabolism | Mutation | S-Adenosylmethionine - metabolism | Amino Acid Substitution | Enzymology
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6. Full Text Heterofunctional Magnetic Metal‐Chelate‐Epoxy Supports for the Purification and Covalent Immobilization of Benzoylformate Decarboxylase From Pseudomonas Putida and Its Carboligation Reactivity
by Tural, Servet and Tural, Bilsen and Demir, Ayhan S
Chirality, ISSN 0899-0042, 09/2015, Volume 27, Issue 9, pp. 635 - 642
In this study, the combined use of the selectivity of metal chelate affinity chromatography with the capacity of epoxy supports to immobilize poly‐His‐tagged... 
one step purification | metal‐affinity magnetic nanoparticles | selective immobilization | covalent attachment | immobilized benzoylformate decarboxylase | metal‐chelate‐epoxy magnetic support | metal-chelate-epoxy magnetic support | metal-affinity magnetic nanoparticles | CHEMISTRY, ANALYTICAL | CHEMISTRY, MEDICINAL | ENANTIOSELECTIVE SYNTHESIS | C BOND FORMATION | ACTIVATED SUPPORTS | CHEMISTRY, ORGANIC | ASPERGILLUS-ORYZAE | ENZYME IMMOBILIZATION | ADDITIONAL STABILIZATION | PROTEIN IMMOBILIZATION | SALT-INDUCED IMMOBILIZATION | BETA-GALACTOSIDASE | SILICA NANOPARTICLES | PHARMACOLOGY & PHARMACY | Acetaldehyde - chemistry | Acetone - chemistry | Enzymes, Immobilized - chemistry | Enzymes, Immobilized - metabolism | Acetone - analogs & derivatives | Benzaldehydes - chemistry | Biocatalysis | Acetone - chemical synthesis | Stereoisomerism | Chelating Agents - chemistry | Benzoin - chemistry | Magnets - chemistry | Enzymes, Immobilized - isolation & purification | Pseudomonas putida - enzymology | Carboxy-Lyases - chemistry | Carboxy-Lyases - isolation & purification | Epoxy Compounds - chemistry | Carboxy-Lyases - metabolism | Histidine - chemistry | Cobalt - chemistry | Enzymes | Epoxy resins | Covalence | Chelating | Purification | Chirality | Immobilization | Density | Recombinant
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7. Full Text A natural protecting group strategy to carry an amino acid starter unit in the biosynthesis of macrolactam polyketide antibiotics
by Shinohara, Yuji and Kudo, Fumitaka and Eguchi, Tadashi
Journal of the American Chemical Society, ISSN 0002-7863, 11/2011, Volume 133, Issue 45, pp. 18134 - 18137
Macrolactam antibiotics are an important class of macrocyclic polyketides that contain a unique nitrogen-containing starter unit. In the present study, a set... 
ADENYLATION DOMAINS | VICENISTATIN | PATHWAY | BUTIROSIN | CHEMISTRY, MULTIDISCIPLINARY | SIDE-CHAIN | Stereoisomerism | Molecular Conformation | Amino Acids - chemistry | Ligases - metabolism | Aminoglycosides - chemistry | Carboxy-Lyases - chemistry | Ligases - chemistry | Intramolecular Transferases - metabolism | Macrolides - chemistry | Anti-Bacterial Agents - chemistry | Aminoglycosides - biosynthesis | Anti-Bacterial Agents - biosynthesis | Carboxy-Lyases - metabolism | Intramolecular Transferases - chemistry | Lactams - chemistry
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8. Full Text New tricks for the glycyl radical enzyme family
by Backman, Lindsey R. F and Funk, Michael A and Dawson, Christopher D and Drennan, Catherine. L
Critical Reviews in Biochemistry and Molecular Biology, ISSN 1040-9238, 11/2017, Volume 52, Issue 6, pp. 674 - 695
Glycyl radical enzymes (GREs) are important biological catalysts in both strict and facultative anaerobes, playing key roles both in the human microbiota and... 
class III ribonucleotide reductase | anaerobic metabolism | Glycyl radical enzymes | radical decarboxylases | pyruvate formate-lyase | choline trimethylamine-lyase | radical chemistry | benzylsuccinate synthase | ETHANOLAMINE AMMONIA-LYASE | BIOCHEMISTRY & MOLECULAR BIOLOGY | ESCHERICHIA-COLI | AROMATICA STRAIN T1 | ANAEROBIC RIBONUCLEOTIDE REDUCTASE | IN-VITRO CHARACTERIZATION | THAUERA-AROMATICA | ACTIVATING ENZYME | Anaerobiosis | Acetyltransferases - metabolism | Bacteria - metabolism | Bacteria - chemistry | Ribonucleotide Reductases - chemistry | Humans | Bacterial Proteins - chemistry | Ligases - metabolism | Models, Molecular | Substrate Specificity | Sugar Alcohol Dehydrogenases - chemistry | Carboxy-Lyases - chemistry | Ligases - chemistry | Fermentation | Acetyltransferases - chemistry | Microbiota | Ribonucleotide Reductases - metabolism | Bacterial Proteins - metabolism | Protein Conformation | Carboxy-Lyases - metabolism | Sugar Alcohol Dehydrogenases - metabolism | glycyl radical enzymes
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9. Full Text A Trivalent Enzymatic System for Uricolytic Therapy of HPRT Deficiency and Lesch-Nyhan Disease
by Ronda, Luca and Marchetti, Marialaura and Piano, Riccardo and Liuzzi, Anastasia and Corsini, Romina and Percudani, Riccardo and Bettati, Stefano
Pharmaceutical Research, ISSN 0724-8741, 07/2017, Volume 34, Issue 7, pp. 1477 - 1490
Purpose Because of the evolutionary loss of the uricolytic pathway, humans accumulate poorly soluble urate as the final product of purine catabolism.... 
enzyme therapy | hyperuricemia | polyethylene glycol | purine degradation | gout | Lesch-Nyhan disease | THERMAL-STABILITY | URATE OXIDASE | PROTEIN | PEGLOTICASE | POLYMER CONJUGATION | CHEMISTRY, MULTIDISCIPLINARY | URIC-ACID DEGRADATION | TETRAMER DISSOCIATION | IN-VIVO | PHARMACOLOGY & PHARMACY | PEGYLATION | Enzyme Therapy | Uricosuric Agents - chemistry | Allantoin - chemistry | Molecular Weight | Stereoisomerism | Humans | Solubility | Recombinant Proteins - chemistry | Lesch-Nyhan Syndrome - drug therapy | Polyethylene Glycols - chemistry | Zebrafish | Carboxy-Lyases - chemistry | Amidohydrolases - chemistry | Hyperuricemia - drug therapy | Hypoxanthine Phosphoribosyltransferase - deficiency | Uric Acid - chemistry | Animals | Urate Oxidase - chemistry | Purines | Enzymes | Alkaloids | Biological products | Metabolites | Polyethylene glycol | Polyols | Therapy | Stability | Allantoin | In vitro testing | Uric acid | Conversion | Guanine | Hyperuricemia | Lesch-Nyhan syndrome | Enzymatic activity | Restoration | Hypoxanthine | Phosphoribosyltransferase | Catabolism | Conjugation | Freeze-drying | Recombinant | Research Paper
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10. Full Text Mechanistic Studies of the Radical S- Adenosyl- l -methionine Enzyme 4-Demethylwyosine Synthase Reveal the Site of Hydrogen Atom Abstraction
by Young, Anthony P and Bandarian, Vahe
Biochemistry, ISSN 0006-2960, 06/2015, Volume 54, Issue 23, pp. 3569 - 3572
TYW1 catalyzes the formation of 4-demethylwyosine via the condensation of N-methylguanosine (m(1)G) with carbons 2 and 3 of pyruvate. In this study, labeled... 
NUCLEOSIDE | BASE FORMATION | PYRUVATE | CRYSTAL-STRUCTURE | BIOSYNTHESIS | BIOCHEMISTRY & MOLECULAR BIOLOGY | SUPERFAMILY | TRANSFER-RNA | WYBUTOSINE | CLUSTER | SAM | Deuterium | Pyruvic Acid - chemistry | RNA, Transfer, Phe - chemistry | Stereoisomerism | RNA, Archaeal - chemistry | Archaeal Proteins - chemistry | S-Adenosylmethionine - chemistry | Iron-Sulfur Proteins - chemistry | Methanococcus - enzymology | Guanosine - chemistry | Free Radicals - metabolism | Pyruvic Acid - metabolism | Carboxy-Lyases - metabolism | Archaeal Proteins - metabolism | Guanosine - analogs & derivatives | RNA, Transfer, Phe - metabolism | Catalytic Domain | Biocatalysis | Free Radicals - chemistry | Models, Molecular | Carboxy-Lyases - chemistry | Guanosine - metabolism | RNA, Archaeal - metabolism | Iron-Sulfur Proteins - metabolism | Methylation | S-Adenosylmethionine - metabolism | Carbon Radioisotopes | Pyruvates | Research | Chemical properties | Hydrogen | Transfer RNA
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11. Full Text Development of a donor-acceptor concept for enzymatic cross-coupling reactions of aldehydes: The first asymmetric cross-benzoin condensation
by Dünkelmann, Pascal and Kolter-Jung, Doris and Nitsche, Adam and Demir, Ayhan S and Siegert, Petra and Lingen, Bettina and Baumann, Martin and Pohl, Martina and Müller, Michael
Journal of the American Chemical Society, ISSN 0002-7863, 10/2002, Volume 124, Issue 41, pp. 12084 - 12085
Highly enantioenriched mixed benzoins are obtained selectively through a biocatalytical cross-coupling reaction of aromatic aldehydes using ThDP-dependent... 
BENZOYLFORMATE DECARBOXYLASE | CATALYST | CHEMISTRY, MULTIDISCIPLINARY | HYDROXY KETONES | Aldehyde-Lyases - chemistry | Benzoin - chemical synthesis | Benzaldehydes - chemistry | Benzoin - analogs & derivatives | Benzoin - chemistry | Carboxy-Lyases - chemistry | Catalysis | Kinetics | Chemical reactions | Research | Chemical properties | Aldehydes | Electron donor-acceptor complexes | Enzymatic analysis
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12. Full Text The UbiX-UbiD system: The biosynthesis and use of prenylated flavin (prFMN)
by Marshall, Stephen A and Payne, Karl A.P and Leys, David
Archives of Biochemistry and Biophysics, ISSN 0003-9861, 10/2017, Volume 632, pp. 209 - 221
The UbiX-UbiD system consists of the flavin prenyltransferase UbiX that produces prenylated FMN that serves as the cofactor for the (de)carboxylase UbiD.... 
Prenylated FMN | UbiD | (de)Carboxylase | Cycloaddition | UbiX | Prenyl transferase | FERULIC ACID DECARBOXYLASE | CRYSTAL-STRUCTURE | BIOCHEMISTRY & MOLECULAR BIOLOGY | INITIAL REACTION | SORBIC ACID | BIOPHYSICS | 4+2 CYCLOADDITION | ESCHERICHIA-COLI K-12 | UBIQUINONE BIOSYNTHESIS | PHENOL METABOLISM | ANAEROBIC METABOLISM | VANILLIC ACID | Flavoproteins - chemistry | Prenylation - physiology | Flavoproteins - metabolism | Flavoproteins - genetics | Flavins - genetics | Escherichia coli Proteins - metabolism | Carboxy-Lyases - chemistry | Escherichia coli - chemistry | Carboxy-Lyases - genetics | Dimethylallyltranstransferase - genetics | Escherichia coli - genetics | Escherichia coli - metabolism | Dimethylallyltranstransferase - metabolism | Escherichia coli Proteins - genetics | Flavins - chemistry | Carboxy-Lyases - metabolism | Escherichia coli Proteins - chemistry | Dimethylallyltranstransferase - chemistry | Flavins - biosynthesis | Physiological aspects | Schiff bases | Enzymes | Usage | Analysis
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13. Full Text A Three‐Enzyme Pathway with an Optimised Geometric Arrangement to Facilitate Substrate Transfer
by Liu, Minghui and Fu, Jinglin and Qi, Xiaodong and Wootten, Shaun and Woodbury, Neal W and Liu, Yan and Yan, Hao
ChemBioChem, ISSN 1439-4227, 06/2016, Volume 17, Issue 12, pp. 1097 - 1101
Cascade reactions drive and regulate a variety of metabolic activities. Efficient coupling of substrate transport between enzymes is important for overall... 
self-assembly | DNA nanostructures | malic dehydrogenase | enzyme cascade | Malic dehydrogenase | Self-assembly | Enzyme cascade | CHEMISTRY, MEDICINAL | ORIGAMI | MALATE-DEHYDROGENASE | MOLECULE | BIOCHEMISTRY & MOLECULAR BIOLOGY | COMPLEXES | ARRAYS | ENZYME | SCAFFOLDS | NANOWIRES | LATTICE | Enzymes - chemistry | L-Lactate Dehydrogenase - metabolism | Malate Dehydrogenase - metabolism | Oxidation-Reduction | Substrate Specificity | Carboxy-Lyases - chemistry | DNA - metabolism | Thermodynamics | DNA - chemistry | L-Lactate Dehydrogenase - chemistry | Nanostructures - chemistry | Carboxy-Lyases - metabolism | Malate Dehydrogenase - chemistry | Enzymes - metabolism | Genetic research | Enzymes
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14. Full Text Biosynthesis of t-Butyl in Apratoxin A: Functional Analysis and Architecture of a PKS Loading Module
by Skiba, Meredith A and Sikkema, Andrew P and Moss, Nathan A and Lowell, Andrew N and Su, Min and Sturgis, Rebecca M and Gerwick, Lena and Gerwick, William H and Sherman, David H and Smith, Janet L
ACS Chemical Biology, ISSN 1554-8929, 06/2018, Volume 13, Issue 6, pp. 1640 - 1650
The unusual feature of a t-butyl group is found in several marine-derived natural products including apratoxin A, a Sec61 inhibitor produced by the... 
DECARBOXYLASE | METHYLATION | POTENT | METHYLTRANSFERASE | POLYKETIDE SYNTHASE | CRYSTAL-STRUCTURE | CARRIER DOMAINS | BIOCHEMISTRY & MOLECULAR BIOLOGY | CYANOBACTERIUM LYNGBYA-MAJUSCULA | MASS-SPECTROMETRY | MARINE NATURAL-PRODUCTS | Amino Acid Sequence | Methyltransferases - chemistry | Catalytic Domain | Multifunctional Enzymes - chemistry | Acyl Carrier Protein - metabolism | Cyanobacteria - chemistry | Methyltransferases - metabolism | Bacterial Proteins - chemistry | Substrate Specificity | Depsipeptides - isolation & purification | Depsipeptides - biosynthesis | Carboxy-Lyases - chemistry | Multifunctional Enzymes - metabolism | Polyketide Synthases - chemistry | Polyketide Synthases - metabolism | Decarboxylation | Bacterial Proteins - metabolism | Carboxy-Lyases - metabolism | Methylation | Depsipeptides - chemistry
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15. Full Text Investigation of anticapsin biosynthesis reveals a four-enzyme pathway to tetrahydrotyrosine in Bacillus subtilis
by Mahlstedt, Sarah A and Walsh, Christopher T
Biochemistry, ISSN 0006-2960, 02/2010, Volume 49, Issue 5, pp. 912 - 923
Bacillus subtilis produces the antibiotic anticapsin as an L-Ala-L-anticapsin dipeptide precursor known as bacilysin, whose synthesis is encoded by the bacA-D... 
REVISION | ANTIBIOTICS | TRANSPORT | ACID | PEPTIDES | MUTASE-PREPHENATE DEHYDRATASE | BIOCHEMISTRY & MOLECULAR BIOLOGY | ESCHERICHIA-COLI | CONFIGURATION | BACILYSIN | TETAINE | Amino Acids, Aromatic - biosynthesis | Carbon-Carbon Double Bond Isomerases - biosynthesis | Cyclohexenes - chemistry | Bacterial Proteins - chemistry | Oxidoreductases Acting on CH-CH Group Donors - biosynthesis | Alanine - chemistry | Transaminases - chemistry | Tyrosine - analogs & derivatives | Alanine - analogs & derivatives | Carbon-Carbon Double Bond Isomerases - chemistry | Alanine - biosynthesis | Amino Acids, Aromatic - chemistry | Amino Acids, Dicarboxylic - chemistry | Tyrosine - chemistry | Transaminases - biosynthesis | Prephenate Dehydratase - biosynthesis | Bacillus subtilis - enzymology | Carboxy-Lyases - chemistry | Dipeptides - chemistry | Oxidoreductases Acting on CH-CH Group Donors - chemistry | Carboxy-Lyases - biosynthesis | Carbon-Carbon Double Bond Isomerases - genetics | Signal Transduction - physiology | Bacterial Proteins - biosynthesis | Cyclohexanecarboxylic Acids - chemistry | Bacillus subtilis | Epoxy compounds | Physiological aspects | Genetic aspects | Chemical properties | Oxidoreductases | Cyclohexanol
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16. Full Text Formation of Hexacoordinate Mn(III) in Bacillus subtilis Oxalate Decarboxylase Requires Catalytic Turnover
by Zhu, Wen and Wilcoxen, Jarett and Britt, R. David and Richards, Nigel G. J
Biochemistry, ISSN 0006-2960, 01/2016, Volume 55, Issue 3, pp. 429 - 434
Oxalate decarboxylase (OxDC) catalyzes the disproportionation of oxalic acid monoanion into CO2 and formate. The enzyme has long been hypothesized to utilize... 
IDENTITY | DIOXYGEN | COMPLEX | ACTIVATION | ACTIVE-SITE | MANGANESE | EPR | BIOCHEMISTRY & MOLECULAR BIOLOGY | COORDINATION | CENTERS | SUPEROXIDE-DISMUTASE | Oxalates - chemistry | Biocatalysis | Electron Spin Resonance Spectroscopy | Oxidation-Reduction | Bacterial Proteins - chemistry | Oxygen - chemistry | Recombinant Proteins - chemistry | Bacillus subtilis - enzymology | Carboxy-Lyases - chemistry | Manganese - chemistry | Coordination Complexes - chemistry | Hydrogen-Ion Concentration | Usage | Bacillus subtilis | Electron paramagnetic resonance spectroscopy | Research | Chemical properties | Oxalates | Decarboxylases | Manganese
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17. Full Text Thiamin diphosphate in biological chemistry: exploitation of diverse thiamin diphosphate‐dependent enzymes for asymmetric chemoenzymatic synthesis
by Müller, Michael and Gocke, Dörte and Pohl, Martina
The FEBS Journal, ISSN 1742-464X, 06/2009, Volume 276, Issue 11, pp. 2894 - 2904
Thiamin diphosphate‐dependent enzymes participate in numerous biosynthetic pathways and catalyse a broad range of reactions, mainly involving the cleavage and... 
2‐hydroxy ketones | screening | selection | benzoin condensation | stereochemistry | catalysis | benzaldehyde lyase | thiamin diphosphate chemistry | carbon–carbon ligation | pyruvate decarboxylases | Screening | Selection | Pyruvate decarboxylases | Catalysis | Stereochemistry | Benzoin condensation | Carbon-carbon ligation | Thiamin diphosphate chemistry | 2-hydroxy ketones | Benzaldehyde lyase | C-BOND FORMATION | carbon-carbon ligation | PSEUDOMONAS-PUTIDA | CRYSTAL-STRUCTURE