Efficient removal of toxic phthalate by immobilized serine-type aldehyde-tagged esterase G

Sungkeeree, Pareenart; Whangsuk, Wirongrong; Sallabhan, Ratiboot; Dubbs, James M.; Mongkolsuk, Skorn; Loprasert, Suvit

doi:10.1016/j.procbio.2017.09.009

Cited by 9 publications

(8 citation statements)

References 28 publications

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“…[19][20][21][22] In addition, the iron-sulfur protein AtsB of the radical S-adenosyl methionine (radical-SAM) protein superfamily is another FGly-generating system that is exclusively found in prokaryotes. [29][30][31][32] This aldehyde-tag methodology has been proven highly efficient for the generation of site-specific ADCs with defined antibody/drug ratios. [29][30][31][32] This aldehyde-tag methodology has been proven highly efficient for the generation of site-specific ADCs with defined antibody/drug ratios.…”

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confidence: 99%

“…[23][24][25][26][27][28] Unlike FGE, AtsB oxygen-independently catalyzes FGly formation with ab roader substrate scope,a lso accepting proline-free motifs and even serine for FGly generation (Figure 1a). [29][30][31][32] This aldehyde-tag methodology has been proven highly efficient for the generation of site-specific ADCs with defined antibody/drug ratios. [1,[33][34][35][36] However,t he introduction of different payloads remains achallenge.Inorder to overcome this problem, we present an ew aldehyde-tag method that makes use of two different recognition sequences that are selectively addressed by different formylglycine-generating enzymes.W ea lso present the isolation of AtsB from Methanosarcina mazei (MM-AtsB), and its characterization and application in bioconjugation.…”

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confidence: 99%

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Two‐fold Bioorthogonal Derivatization by Different Formylglycine‐Generating Enzymes

et al. 2018

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Formylglycine-generating enzymes are of increasing interest in the field of bioconjugation chemistry. They catalyze the site-specific oxidation of a cysteine residue to the aldehyde-containing amino acid C -formylglycine (FGly). This non-canonical residue can be generated within any desired target protein and can subsequently be used for bioorthogonal conjugation reactions. The prototypic formylglycine-generating enzyme (FGE) and the iron-sulfur protein AtsB display slight variations in their recognition sequences. We designed specific tags in peptides and proteins that were selectively converted by the different enzymes. Combination of the different tag motifs within a single peptide or recombinant protein enabled the independent and consecutive introduction of two formylglycine residues and the generation of heterobifunctionalized protein conjugates.

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Two‐fold Bioorthogonal Derivatization by Different Formylglycine‐Generating Enzymes

et al. 2018

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“…Thus, inspired by previous studies on serine modification by AtsB, we were interested in the capability of AtsB from Klebsiella pneumoniae (KP‐AtsB) and the anaerobic archaebacterium Methanosarcina mazei (MM‐AtsB) to convert serine‐containing recognition motifs of the SX(P/A)XR‐type in vitro, to achieve further orthogonality to classical cysteine‐containing aldehyde tags.…”

Section: Methodsmentioning

confidence: 99%

“…In these peptides, two serine‐containing recognition sequences were chosen. First, the SAPAR motif from K. pneumoniae sulfatase, which is the endogenous substrate of KP‐AtsB . Second, the STAGR motif, which carries a substitution of cysteine by serine within the M. mazei sulfatase sequence CTAGR, that is, the natural substrate of MM‐AtsB.…”

Section: Methodsmentioning

confidence: 99%

Conversion of Serine‐Type Aldehyde Tags by the Radical SAM Protein AtsB from Methanosarcina mazei

et al. 2019

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Formylglycine‐generating enzymes provide a convenient tool for site‐specific protein derivatization. Their ability to oxidize cysteine or serine residues within a defined consensus sequence to Cα‐formylglycine (FGly) allows for the targeted introduction of a unique chemical handle for various bioconjugation reactions. In recent years, oxygen‐dependent FGly‐generating enzyme saw broad use in protein functionalization and the generation of protein conjugates. Yet, the FGly‐generating system AtsB, along with its capability to convert unusual aldehyde tag sequences, remains mostly unused. Herein, the ability of AtsB from Methanosarcina mazei to convert nonclassical aldehyde tags of the SX(A/P)XR‐type and its potential use in bioconjugation chemistry are demonstrated.

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“…Es gehört zur Radikal‐SAM‐Proteinsuperfamilie (SAM= S ‐Adenosylmethionin) und kommt ausschließlich in Prokaryoten vor. Anders als FGE bildet es FGly in einem Sauerstoff‐unabhängigen Mechanismus und verfügt über ein breiteres Substratspektrum, wobei auch Prolin‐freie Motive oder Serin statt Cystein zur FGly‐Bildung akzeptiert werden (Abbildung a) …”

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Zweifach‐bioorthogonale Derivatisierung durch verschiedene Formylglycin‐generierende Enzyme

et al. 2018

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Formylglycin-generierende Enzyme haben in den letzten Jahren breite Anwendung in der bioorthogonalen Chemie gefunden. Sie katalysieren die ortsspezifische Oxidation eines Cysteinrestes zur Aldehyd-haltigen Aminosäure C a -Formylglycin (FGly). FGly kann in jedem beliebigen Zielprotein generiert und anschließend fürb ioorthogonale Konjugationsreaktionen genutzt werden. Das prototypische Formylglycin-generierende Enzym (FGE) und das Eisen-Schwefel-Protein AtsB zeigen leichte Variationen in ihren Erkennungssequenzen. Spezifische Motive in Peptiden und Proteinen wurden entworfen, die selektiv von diesen Enzymen adressiert werden. Die Kombination dieser Motive innerhalb eines Peptids oder rekombinanten Proteins ermçglichte die unabhängige und sukzessive Einführung von zwei FGly-Resten und die Generierung hetero-difunktionalisierter Proteinkonjugate.

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Efficient removal of toxic phthalate by immobilized serine-type aldehyde-tagged esterase G

Cited by 9 publications

References 28 publications

Two‐fold Bioorthogonal Derivatization by Different Formylglycine‐Generating Enzymes

Two‐fold Bioorthogonal Derivatization by Different Formylglycine‐Generating Enzymes

Conversion of Serine‐Type Aldehyde Tags by the Radical SAM Protein AtsB from Methanosarcina mazei

Zweifach‐bioorthogonale Derivatisierung durch verschiedene Formylglycin‐generierende Enzyme

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