Sequence and properties of pentaerythritol tetranitrate reductase from Enterobacter cloacae PB2
about
Distribution and Fate of Military Explosives and Propellants in Soil: A ReviewBiological degradation of 2,4,6-trinitrotolueneThe flavoproteome of the yeast Saccharomyces cerevisiaeThe role of glutamine 114 in old yellow enzymeKinetic and structural basis of reactivity of pentaerythritol tetranitrate reductase with NADPH, 2-cyclohexenone, nitroesters, and nitroaromatic explosivesCrystal structure of bacterial morphinone reductase and properties of the C191A mutant enzymeFocused directed evolution of pentaerythritol tetranitrate reductase by using automated anaerobic kinetic screening of site-saturated librariesA site-saturated mutagenesis study of pentaerythritol tetranitrate reductase reveals that residues 181 and 184 influence ligand binding, stereochemistry and reactivityOn the active site of Old Yellow Enzyme. Role of histidine 191 and asparagine 194Gene cloning and nucleotide sequencing and properties of a cocaine esterase from Rhodococcus sp. strain MB1Comparative structural modeling of six old yellow enzymes (OYEs) from the necrotrophic fungus Ascochyta rabiei: insight into novel OYE classes with differences in cofactor binding, organization of active site residues and stereopreferencesPurification, properties, and sequence of glycerol trinitrate reductase from Agrobacterium radiobacter.Thermoregulated expression and characterization of an NAD(P)H-dependent 2-cyclohexen-1-one reductase in the plant pathogenic bacterium Pseudomonas syringae pv. glycinea.Aerobic degradation of 2,4,6-trinitrotoluene by Enterobacter cloacae PB2 and by pentaerythritol tetranitrate reductase.Transformation of 2,4,6-trinitrotoluene by purified xenobiotic reductase B from Pseudomonas fluorescens I-C.Biotransformations of explosives.Structure of the inhibitor complex of old yellow enzyme from Trypanosoma cruziBiodegradation, biotransformation, and biocatalysis (b3)Regioselectivity of nitroglycerin denitration by flavoprotein nitroester reductases purified from two Pseudomonas species.A key role for old yellow enzyme in the metabolism of drugs by Trypanosoma cruziPreparation, crystallization and preliminary crystallographic analysis of old yellow enzyme from Trypanosoma cruziOld yellow enzyme: reduction of nitrate esters, glycerin trinitrate, and propylene 1,2-dinitrate.Comprehensive genome-wide analysis reveals different classes of enigmatic old yellow enzyme in fungiArabidopsis and the genetic potential for the phytoremediation of toxic elemental and organic pollutants.Asymmetric bioreduction of activated alkenes to industrially relevant optically active compounds.Carbon-carbon double-bond reductases in nature.Harnessing microbial gene pools to remediate persistent organic pollutants using genetically modified plants--a viable technology?Complete denitration of nitroglycerin by bacteria isolated from a washwater soakaway.Structure-Based Insight into the Asymmetric Bioreduction of the C=C Double Bond of alpha,beta-Unsaturated Nitroalkenes by Pentaerythritol Tetranitrate Reductase.Asymmetric Reduction of Activated Alkenes by Pentaerythritol Tetranitrate Reductase: Specificity and Control of Stereochemical Outcome by Reaction Optimisation.Characterization of glycerol trinitrate reductase (NerA) and the catalytic role of active-site residues.Biotransformation of explosives by the old yellow enzyme family of flavoproteins.Nicotinamide-independent asymmetric bioreduction of CC-bonds via disproportionation of enones catalyzed by enoate reductases.Engineering towards nitroreductase functionality in ene-reductase scaffolds.Comparative characterization and expression analysis of the four Old Yellow Enzyme homologues from Shewanella oneidensis indicate differences in physiological function.Understanding the broad substrate repertoire of nitroreductase based on its kinetic mechanism.Key enzymes enabling the growth of Arthrobacter sp. strain JBH1 with nitroglycerin as the sole source of carbon and nitrogen.Nanofibrillar Peptide hydrogels for the immobilization of biocatalysts for chemical transformations.Bioreduction of alpha-methylcinnamaldehyde derivatives: chemo-enzymatic asymmetric synthesis of Lilial and Helional.Ligand-induced conformational changes in the capping subdomain of a bacterial old yellow enzyme homologue and conserved sequence fingerprints provide new insights into substrate binding.
P2860
Q21285017-DCB4156F-662D-4E4A-8BE7-42759C4421D3Q24548467-E83D8D3A-2181-408D-85D4-88F72DC5E632Q27021669-318EBE8F-B6F8-4AB8-B680-90B5E711926FQ27635468-E3FAC9F1-331C-4C35-BB70-0C05B400640FQ27638657-8EBB3EA3-509B-48A0-9ACD-BACC69D835C2Q27639077-1E54D091-D17C-4949-B007-732445DE3A7BQ27665727-6AF1785C-58C0-4F39-9570-C11FD3839660Q27666872-341CD53C-44B8-4E9D-B281-0FF186CB66DFQ27766083-E546D2FB-E466-47D2-AA50-2698B4FCEE2DQ28343986-E554A56E-0867-4934-89E7-187901D634E7Q28538270-930EAEA2-F581-452E-8FD3-CCFAF6B7ECDDQ30176349-6F10A821-E61F-42EB-9E7E-892A6AC6B598Q31919153-43F087D1-5D1D-432A-853E-68AFD36F4511Q33721405-DB383A85-6C7C-49BA-AAE8-357B41F693ADQ33988003-E00AFDFD-13B7-4131-ADEE-269DE7B1CDBFQ34351836-FA8F641B-B20A-47EB-A5BC-5E6427628833Q34416239-750595FF-838F-47F4-9AF2-EF46C57C5003Q34905240-AC4A0FC7-B113-46B5-8521-50916E98D753Q35632223-F66A5896-BE41-43D9-824E-85C426769AEDQ36371444-2783514A-E80B-4D82-BA88-C38F289219BFQ36588449-63CF47FB-2E1A-49EA-8735-8CCF191A39FDQ37105411-0A11AF6C-7A12-43EB-91F1-A651142868D7Q37559667-D9A512CE-8A33-4C76-A78E-0D08554EB9EEQ37981152-7AD67DE0-0329-4E54-A597-0DBF5ABE23C0Q38002231-1827E06D-1604-4D6D-A632-4E8A0B81793FQ38205904-CBBAC09C-7381-467F-9C37-88FEC3DBDD0CQ38568666-0AD28832-684F-41E4-8DA1-0C06D87A7F80Q39491237-AE9BAFAF-D3F7-48A3-ACF2-FA442D6A70C2Q40024861-FB17EA5B-E9EF-40DB-9E4A-4CE19B8A2583Q40025162-02FBEEF0-9803-49B7-883D-76D4ACDD178CQ40634223-42D21AE6-0AE0-44C1-84DB-F58C6D03DEC4Q40937713-CF2B0A94-E6C9-490F-A61A-C5DA33E06227Q41378442-726CEA0A-607C-4442-8DFC-CC1A8542ECD6Q41378518-20196797-54FA-40BA-AE5C-09DB800284BCQ41867200-39E3A2DA-59C9-4AFA-B21E-14AA24D55F24Q41942807-7F11E614-9D58-47F3-98D4-367977D1E9CEQ41960802-941DFF8F-BD7F-4807-B7C6-831259FB6552Q41998666-25A30DDB-48EC-473C-9D1A-A0824192BF2DQ42166307-49315BE4-4042-46BB-B330-0FAB3783E701Q42692245-C1F85DF3-F38F-475B-BF3F-DB2D99B96661
P2860
Sequence and properties of pentaerythritol tetranitrate reductase from Enterobacter cloacae PB2
description
1996 nî lūn-bûn
@nan
1996 թուականի Նոյեմբերին հրատարակուած գիտական յօդուած
@hyw
1996 թվականի նոյեմբերին հրատարակված գիտական հոդված
@hy
1996年の論文
@ja
1996年論文
@yue
1996年論文
@zh-hant
1996年論文
@zh-hk
1996年論文
@zh-mo
1996年論文
@zh-tw
1996年论文
@wuu
name
Sequence and properties of pen ...... from Enterobacter cloacae PB2
@ast
Sequence and properties of pen ...... from Enterobacter cloacae PB2
@en
Sequence and properties of pen ...... from Enterobacter cloacae PB2
@nl
type
label
Sequence and properties of pen ...... from Enterobacter cloacae PB2
@ast
Sequence and properties of pen ...... from Enterobacter cloacae PB2
@en
Sequence and properties of pen ...... from Enterobacter cloacae PB2
@nl
prefLabel
Sequence and properties of pen ...... from Enterobacter cloacae PB2
@ast
Sequence and properties of pen ...... from Enterobacter cloacae PB2
@en
Sequence and properties of pen ...... from Enterobacter cloacae PB2
@nl
P2093
P2860
P1476
Sequence and properties of pen ...... from Enterobacter cloacae PB2
@en
P2093
P2860
P304
P356
10.1128/JB.178.22.6623-6627.1996
P407
P577
1996-11-01T00:00:00Z