Characterization of Arylsulfatase Formed by Derepressed Synthesis in<i>Citrobacter braakii</i>

Miura, Toyokazu; Okamoto, Kenji; Yanase, Hideshi

doi:10.1271/bbb.50651

Cited by 5 publications

(2 citation statements)

References 10 publications

(8 reference statements)

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“…18,31 We use substrates 1-4 to assign a function to sub-groups of the superfamily (e.g. potentially as phosphate monoesterases, phosphodiesterases, 30 phosphonate monoester hydrolases, 32 or arylsulfatases, [33][34][35][36] ), leading to classification of newly identified enzymes according to their respective top activity, even though the natural substrates may not be known.…”

Section: Introductionmentioning

confidence: 99%

“…The reactions catalyzed by these enzymes are thermodynamically demanding, with half-lives ranging from 200 days to 10 5 years. The AP superfamily is characterized by crosswise catalytic promiscuity, that is, the “primary” reactions of one enzyme are found to be promiscuous reactions catalyzed by other family members ,,,,− ,, (Figure ) as well as additional activities. , We use substrates 1 – 4 to assign a function to subgroups of the superfamily (e.g., potentially as phosphate monoesterases, phosphodiesterases, phosphonate monoester hydrolases, or arylsulfatases, − ), leading to classification of newly identified enzymes according to their respective top activity, even though the natural substrates may not be known.…”

Section: Introductionmentioning

confidence: 99%

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Balancing Specificity and Promiscuity in Enzyme Evolution: Multidimensional Activity Transitions in the Alkaline Phosphatase Superfamily

et al. 2018

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Highly proficient, promiscuous enzymes can be springboards for functional evolution, able to avoid loss of function during adaptation by their capacity to promote multiple reactions. We employ systematic comparative study of structure, sequence and substrate specificity to track the evolution of specificity and reactivity between promiscuous members of clades of the alkaline phosphatase (AP) superfamily. Construction of a phylogenetic tree of protein sequences maps out the likely transition zone between arylsulfatases (ASs) and phosphonate monoester hydrolases (PMHs). Kinetic analysis shows that all enzymes characterized have four chemically distinct phospho-and sulfoesterase activities, with rate accelerations ranging from 10 11-10 17-fold for their primary and 10 9-10 12-fold for their promiscuous reactions, suggesting that catalytic promiscuity is widespread in the AP-superfamily. This functional characterization and crystallography reveal a novel class of ASs that is so similar in sequence to known PMHs that it had not been recognized as having diverged in function. Based on analysis of snapshots of catalytic promiscuity 'in transition' we develop possible models that would allow functional evolution and determine scenarios for trade-off between multiple activities. For the new ASs we observe largely invariant substrate specificity that would facilitate the transition from ASs to PMHs via trade-off-free molecular exaptation, i.e. evolution without initial loss of primary activity and specificity toward the original substrate. This ability to bypass low activity generalists provides a molecular solution to avoid adaptive conflict.

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Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Balancing Specificity and Promiscuity in Enzyme Evolution: Multidimensional Activity Transitions in the Alkaline Phosphatase Superfamily

et al. 2018

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Detection, production, and application of microbial arylsulfatases

Stressler

Seitl

Kühn

et al. 2016

Appl Microbiol Biotechnol

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Arylsulfatases are enzymes which catalyze the hydrolysis of arylsulfate ester bonds to release a free sulfonate. They are widespread in nature and are found in microorganisms, most animal and human tissues, and plant seeds. However, this review focuses on arylsulfatases from microbial origin and gives an overview of different assays and substrates used to determine the arylsulfatase activity. Furthermore, the production of microbial arylsulfatases using wild-type organisms as well as the recombinant production using Escherichia coli and Kluyveromyces lactis as expression hosts is discussed. Finally, various potential applications of these enzymes are reviewed.

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Detection, production, modification, and application of arylsulfatases

Secundo

et al. 2023

Biotechnology Advances

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Characterization of Arylsulfatase Formed by Derepressed Synthesis inCitrobacter braakii

Cited by 5 publications

References 10 publications

Balancing Specificity and Promiscuity in Enzyme Evolution: Multidimensional Activity Transitions in the Alkaline Phosphatase Superfamily

Balancing Specificity and Promiscuity in Enzyme Evolution: Multidimensional Activity Transitions in the Alkaline Phosphatase Superfamily

Detection, production, and application of microbial arylsulfatases

Detection, production, modification, and application of arylsulfatases

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