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An enzyme-trap approach allows isolation of intermediates in cobalamin biosynthesis

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An enzyme-trap approach allows isolation of intermediates in cobalamin biosynthesis. / Deery, Evelyne; Schroeder, Susanne; Lawrence, Andrew D.; Taylor, Samantha L.; Seyedarabi, Arefeh; Waterman, Jitka; Wilson, Keith S.; Brown, David; Geeves, Michael A.; Howard, Mark J.; Pickersgill, Richard W.; Warren, Martin J.

In: NATURE CHEMICAL BIOLOGY, Vol. 8, No. 11, 11.2012, p. 933-940.

Research output: Contribution to journalArticle

Harvard

Deery, E, Schroeder, S, Lawrence, AD, Taylor, SL, Seyedarabi, A, Waterman, J, Wilson, KS, Brown, D, Geeves, MA, Howard, MJ, Pickersgill, RW & Warren, MJ 2012, 'An enzyme-trap approach allows isolation of intermediates in cobalamin biosynthesis', NATURE CHEMICAL BIOLOGY, vol. 8, no. 11, pp. 933-940. https://doi.org/10.1038/NCHEMBIO.1086

APA

Deery, E., Schroeder, S., Lawrence, A. D., Taylor, S. L., Seyedarabi, A., Waterman, J., ... Warren, M. J. (2012). An enzyme-trap approach allows isolation of intermediates in cobalamin biosynthesis. NATURE CHEMICAL BIOLOGY, 8(11), 933-940. https://doi.org/10.1038/NCHEMBIO.1086

Vancouver

Deery E, Schroeder S, Lawrence AD, Taylor SL, Seyedarabi A, Waterman J et al. An enzyme-trap approach allows isolation of intermediates in cobalamin biosynthesis. NATURE CHEMICAL BIOLOGY. 2012 Nov;8(11):933-940. https://doi.org/10.1038/NCHEMBIO.1086

Author

Deery, Evelyne ; Schroeder, Susanne ; Lawrence, Andrew D. ; Taylor, Samantha L. ; Seyedarabi, Arefeh ; Waterman, Jitka ; Wilson, Keith S. ; Brown, David ; Geeves, Michael A. ; Howard, Mark J. ; Pickersgill, Richard W. ; Warren, Martin J. / An enzyme-trap approach allows isolation of intermediates in cobalamin biosynthesis. In: NATURE CHEMICAL BIOLOGY. 2012 ; Vol. 8, No. 11. pp. 933-940.

Bibtex - Download

@article{dab6a2c4de17456cb6f4bf1a2dc6f2ae,
title = "An enzyme-trap approach allows isolation of intermediates in cobalamin biosynthesis",
abstract = "The biosynthesis of many vitamins and coenzymes has often proven difficult to elucidate owing to a combination of low abundance and kinetic lability of the pathway intermediates. Through a serial reconstruction of the cobalamin (vitamin B-12) pathway in Escherichia coli and by His tagging the terminal enzyme in the reaction sequence, we have observed that many unstable intermediates can be isolated as tightly bound enzyme-product complexes. Together, these approaches have been used to extract intermediates between precorrin-4 and hydrogenobyrinic acid in their free acid form and permitted the delineation of the overall reaction catalyzed by CobL, including the formal elucidation of precorrin-7 as a metabolite. Furthermore, a substrate-carrier protein, CobE, that can also be used to stabilize some of the transient metabolic intermediates and enhance their onward transformation, has been identified. The tight association of pathway intermediates with enzymes provides evidence for a form of metabolite channeling.",
keywords = "RHODOBACTER-CAPSULATUS, PSEUDOMONAS-DENITRIFICANS, PURIFICATION, HYDROGENOBYRINIC ACID, MAXIMUM-LIKELIHOOD, RING CONTRACTION, PRECORRIN-8X, GENE-PRODUCT, VITAMIN-B12 BIOSYNTHESIS, SUBSTRATE",
author = "Evelyne Deery and Susanne Schroeder and Lawrence, {Andrew D.} and Taylor, {Samantha L.} and Arefeh Seyedarabi and Jitka Waterman and Wilson, {Keith S.} and David Brown and Geeves, {Michael A.} and Howard, {Mark J.} and Pickersgill, {Richard W.} and Warren, {Martin J.}",
year = "2012",
month = "11",
doi = "10.1038/NCHEMBIO.1086",
language = "English",
volume = "8",
pages = "933--940",
journal = "NATURE CHEMICAL BIOLOGY",
issn = "1552-4450",
publisher = "Nature Publishing Group",
number = "11",

}

RIS (suitable for import to EndNote) - Download

TY - JOUR

T1 - An enzyme-trap approach allows isolation of intermediates in cobalamin biosynthesis

AU - Deery, Evelyne

AU - Schroeder, Susanne

AU - Lawrence, Andrew D.

AU - Taylor, Samantha L.

AU - Seyedarabi, Arefeh

AU - Waterman, Jitka

AU - Wilson, Keith S.

AU - Brown, David

AU - Geeves, Michael A.

AU - Howard, Mark J.

AU - Pickersgill, Richard W.

AU - Warren, Martin J.

PY - 2012/11

Y1 - 2012/11

N2 - The biosynthesis of many vitamins and coenzymes has often proven difficult to elucidate owing to a combination of low abundance and kinetic lability of the pathway intermediates. Through a serial reconstruction of the cobalamin (vitamin B-12) pathway in Escherichia coli and by His tagging the terminal enzyme in the reaction sequence, we have observed that many unstable intermediates can be isolated as tightly bound enzyme-product complexes. Together, these approaches have been used to extract intermediates between precorrin-4 and hydrogenobyrinic acid in their free acid form and permitted the delineation of the overall reaction catalyzed by CobL, including the formal elucidation of precorrin-7 as a metabolite. Furthermore, a substrate-carrier protein, CobE, that can also be used to stabilize some of the transient metabolic intermediates and enhance their onward transformation, has been identified. The tight association of pathway intermediates with enzymes provides evidence for a form of metabolite channeling.

AB - The biosynthesis of many vitamins and coenzymes has often proven difficult to elucidate owing to a combination of low abundance and kinetic lability of the pathway intermediates. Through a serial reconstruction of the cobalamin (vitamin B-12) pathway in Escherichia coli and by His tagging the terminal enzyme in the reaction sequence, we have observed that many unstable intermediates can be isolated as tightly bound enzyme-product complexes. Together, these approaches have been used to extract intermediates between precorrin-4 and hydrogenobyrinic acid in their free acid form and permitted the delineation of the overall reaction catalyzed by CobL, including the formal elucidation of precorrin-7 as a metabolite. Furthermore, a substrate-carrier protein, CobE, that can also be used to stabilize some of the transient metabolic intermediates and enhance their onward transformation, has been identified. The tight association of pathway intermediates with enzymes provides evidence for a form of metabolite channeling.

KW - RHODOBACTER-CAPSULATUS

KW - PSEUDOMONAS-DENITRIFICANS

KW - PURIFICATION

KW - HYDROGENOBYRINIC ACID

KW - MAXIMUM-LIKELIHOOD

KW - RING CONTRACTION

KW - PRECORRIN-8X

KW - GENE-PRODUCT

KW - VITAMIN-B12 BIOSYNTHESIS

KW - SUBSTRATE

UR - http://www.scopus.com/inward/record.url?scp=84867678721&partnerID=8YFLogxK

U2 - 10.1038/NCHEMBIO.1086

DO - 10.1038/NCHEMBIO.1086

M3 - Article

VL - 8

SP - 933

EP - 940

JO - NATURE CHEMICAL BIOLOGY

JF - NATURE CHEMICAL BIOLOGY

SN - 1552-4450

IS - 11

ER -