Corrigendum to “Crystal Structures of Δ1-Pyrroline-5-Carboxylate Reductase from Human Pathogens Neisseria meningitides and Streptococcus pyogenes” [J. Mol. Biol. (2005) 354, 91–106]

Nocek, B.; Chang, Changsoo; Li, H.; Lezondra, L.; Holzle, D.; Collart, F.; Joachimiak, A.

doi:10.1016/j.jmb.2006.01.082

Cited by 3 publications

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“…In Δ 1 ‐piperideine‐2‐carboxylate/Δ 1 ‐pyrroline‐2‐carboxylate reductase from Pseudomonas syringae the alleged proton donor is His54, the p K a of which is thought to be lowered by interactions with Ser53 and Asp194 as the three residues form a catalytic triad (Scheme , B). In bacterial Δ 1 ‐pyrroline‐5‐carboxylate reductases, the proton is thought to be derived from a serine or threonine residue, although the possibility that substrate protonation occurs by water is not excluded,107 and for the pteridine reductase from Leishmania major a tyrosine residue (Tyr194) has been proposed to be the proton donor 108. In the X‐ray crystal structure of thiazoline reductase from Yersinia enterocolitica , His101 and Tyr128 have been identified as potential proton‐donating residues 98…”

Section: Structural and Mechanistic Aspectsmentioning

confidence: 99%

Biocatalytic Imine Reduction and Reductive Amination of Ketones

2015

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Chiral aminesr epresent ap rominentf unctional group in pharmaceuticals and agrochemicals and are hence attractive targets for asymmetric synthesis.S ince the pharmaceutical industry has identified biocatalysis as av aluablet oolf or synthesising chiral molecules with high enantiomeric excess and under mild reactionc onditions,e nzymatic methods for chiral amine synthesisa re increasing in importance.A mong the strategies available in this context, the asymmetric reductiono fi mines by NAD(P)Hdependent enzymes andt he related reductive amination of ketones have long remained underrepresented. However, recent years have witnessed an impressive progress in the applicationo fn atural or engineered imine-reducing enzymes,s uch as imine reductases,o pine dehydrogenases,a mine dehydrogenases, and artificial metalloenzymes.T his review provides ac omprehensive overview of biocatalytic imine reductiona nd reductive amination of ketones,h ighlightingt he natural roles,s ubstrate scopes,s tructural features, and potential applicationf ields of the involvedenzymes.1I ntroduction 2I mine Reduction in Nature 2. 1I ntroductionChiral amines represent the core structure of am yriad of natural products as well as man-made compounds of public demand, such as pharmaceuticals and agrochemicals (Figure 1). Accordingt o recent estimates,c hiral amine moieties are present in about 40% of active pharmaceutical ingredients (APIs) and 20% of agrochemicals.[1] Moreover, optically pure amines,a mino acids,a nd amino alcohols are frequently employed in chemical synthesis as chiral auxiliariesorr esolving agents.Theirp aramount importance across several chemical disciplines andi ndustrial sectors has made chiral amines anda mino acids attractive targets for asymmetrics ynthesis.E stablished approachesf or their preparation are the stereoselective addition of nucleophiles to imines (including the famous Mannich and Strecker reactions), asymmetric C À Ha mination and hydroamination, and the asymmetric reductiono fe namines and imines,w hich may either be pre-formed or may occur as intermediates in an asymmetric reductive amination process.[2] Metallo-or organocatalytic methodsf or asymmetric imine and enamine reductiona re broadly applied, and intense research efforts are devoted to the improvement of the scope and stereoselectivity of these processes. [2,3] In cases where established asymmetric synthesism ethodsa re inapplicable or fail to provide the desired optical purity, diastereomeric salt crystallisation is still widely used for the classical resolution of racemic amines or for upgrading the enantiomeric excess of an optically enriched product.[2d]Biocatalytic transformationsa re increasingly being recognised as an attractive optionf or the asymmetric synthesiso fc hiral molecules.[4] Particularly in the

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Section: Structural and Mechanistic Aspectsmentioning

confidence: 99%

Biocatalytic Imine Reduction and Reductive Amination of Ketones

2015

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“…KPR belongs to the 6-phosphogluconate dehydrogenase superfamily in the SCOP data base (11,12). Among other enzymes in this superfamily are acetohydroxy acid isomeroreductase (13), short chain L-3-hydroxyacyl-CoA dehydrogenase (14), ⌬ 1 -pyrroline-5-carboxylate reductase (15), and prephenate dehydrogenase (16). The secondary structure of KPR comprises 13 ␣-helices and 11 ␤-strands.…”

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confidence: 99%

Crystal Structure of Escherichia coli Ketopantoate Reductase in a Ternary Complex with NADP+ and Pantoate Bound

Ciulli¹,

Chirgadze

Smith

et al. 2007

Journal of Biological Chemistry

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. This work provides insights into the roles of active site residues and conformational changes in substrate recognition and catalysis, leading to the proposal of a detailed molecular mechanism for KPR activity. Pantothenate (vitamin B 5 ) is the precursor of the 4Ј-phosphopantetheine moiety of coenzyme A and acyl carrier proteins, which play an important role in metabolism and fatty acid biosynthesis (1-3). The biosynthetic pathway for pantothenate has been elucidated in Escherichia coli and other bacteria and is composed of four enzymes. The first two convert ␣-ketoisovalerate to pantoate, then in a separate branch L-aspartate is decarboxylated to produce ␤-alanine. Finally, pantoate and ␤-alanine are condensed together to form pantothenate (4, 5). The pathway is similar in plants and fungi, although they appear to use a different route to ␤-alanine (6). Bioinformatics analysis has identified the pantothenate pathway as a potential antimicrobial target (7). This is supported by recent genetic studies which show that a pantothenate auxotroph of Mycobacterium tuberculosis fails to establish chronic infections in mice (8).Ketopantoate reductase (KPR, 2 EC 1.1.1.169), encoded by the panE gene, is the second enzyme in the pathway and catalyzes the NADPH-dependent reduction of ketopantoate to pantoate. Previous biochemical studies on the Escherichia coli enzyme established that hydride transfer is stereospecific from the pro-S proton of NADPH to the si face of ketopantoate (Scheme 1A), and the reaction equilibrium favors NADP ϩ and pantoate formation (9, 10). Steady-state kinetic and inhibition analysis are consistent with a sequential ordered bi:bi kinetic mechanism (Scheme 1B) in which NADPH binding is followed by ketopantoate binding, and then pantoate release precedes NADP ϩ release (10). The pH dependence of catalysis is consistent with the involvement of a general acid/base in the catalytic mechanism (9, 10). Site-directed mutagenesis implicated Lys 176 and Glu 256 as important for catalysis (9). The crystal structure of the apoenzyme was solved by MatakVinkovic et al. (11) at 1.7 Å of resolution. KPR belongs to the 6-phosphogluconate dehydrogenase superfamily in the SCOP data base (11,12). Among other enzymes in this superfamily are acetohydroxy acid isomeroreductase (13), short chain L-3-hydroxyacyl-CoA dehydrogenase (14), ⌬ 1 -pyrroline-5-carboxylate reductase (15), and prephenate dehydrogenase (16). The secondary structure of KPR comprises 13 ␣-helices and 11 ␤-strands. The enzyme is monomeric with a molecular mass of 34 kDa and is composed of a coenzyme binding domain and a substrate binding domain separated by a large cleft. The N-terminal domain has an ␣␤ Rossmann-type fold featured in many nucleotide-binding proteins, with a glycine-rich region ( 7 GCGALG 12 ) for coenzyme recognition (17). The C-terminal substrate binding domain is composed of 8 ␣-helices and has a core of two long antiparallel helices, which is a common motif within the superfamily. * This work was supported by the Biotechnology an...

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“…When using D-lysine, the aldehyde intermediate was formed in a similar yield to L-lysine but no production of D-pipecolic acid was observed, confirming the high stereoselectivity of He-P5C previously observed for similar reductases. [35][36][37] These conversions were maintained when scaling up L-lysine to 50 mM (Fig. S4B †).…”

Section: Resultsmentioning

confidence: 79%