Stretching exercises - Flexibility in dihydrofolate reductase catalysis

Grover Paul Miller; Stephen J. Benkovic

doi:10.1016/S1074-5521(98)90616-0

Stretching exercises - Flexibility in dihydrofolate reductase catalysis

Grover Paul Miller, Stephen J. Benkovic

Chemistry

Research output: Contribution to journal › Review article › peer-review

102 Scopus citations

Abstract

As an enzyme, dihydrofolate reductase performs two tasks: transformation of its substrate dihydrofolate or folate to tetrahydrofolate, using NADPH as a cofactor, and regeneration of the enzyme for a subsequent round of catalysis. Studies discussed in this review highlight the role of conformational flexibility in both of these enzymatic functions.

Original language	English (US)
Pages (from-to)	R105-R113
Journal	Chemistry and Biology
Volume	5
Issue number	5
DOIs	https://doi.org/10.1016/S1074-5521(98)90616-0
State	Published - May 1998

All Science Journal Classification (ASJC) codes

Biochemistry
Molecular Medicine
Molecular Biology
Pharmacology
Drug Discovery
Clinical Biochemistry

Access to Document

10.1016/S1074-5521(98)90616-0

Cite this

@article{ea163b0a0e2d43928685c0cc48a1423c,

title = "Stretching exercises - Flexibility in dihydrofolate reductase catalysis",

abstract = "As an enzyme, dihydrofolate reductase performs two tasks: transformation of its substrate dihydrofolate or folate to tetrahydrofolate, using NADPH as a cofactor, and regeneration of the enzyme for a subsequent round of catalysis. Studies discussed in this review highlight the role of conformational flexibility in both of these enzymatic functions.",

author = "Miller, \{Grover Paul\} and Benkovic, \{Stephen J.\}",

year = "1998",

month = may,

doi = "10.1016/S1074-5521(98)90616-0",

language = "English (US)",

volume = "5",

pages = "R105--R113",

journal = "Chemistry and Biology",

issn = "1074-5521",

publisher = "Elsevier Inc.",

number = "5",

}

TY - JOUR

T1 - Stretching exercises - Flexibility in dihydrofolate reductase catalysis

AU - Miller, Grover Paul

AU - Benkovic, Stephen J.

PY - 1998/5

Y1 - 1998/5

N2 - As an enzyme, dihydrofolate reductase performs two tasks: transformation of its substrate dihydrofolate or folate to tetrahydrofolate, using NADPH as a cofactor, and regeneration of the enzyme for a subsequent round of catalysis. Studies discussed in this review highlight the role of conformational flexibility in both of these enzymatic functions.

AB - As an enzyme, dihydrofolate reductase performs two tasks: transformation of its substrate dihydrofolate or folate to tetrahydrofolate, using NADPH as a cofactor, and regeneration of the enzyme for a subsequent round of catalysis. Studies discussed in this review highlight the role of conformational flexibility in both of these enzymatic functions.

UR - https://www.scopus.com/pages/publications/0031808658

UR - https://www.scopus.com/inward/citedby.url?scp=0031808658&partnerID=8YFLogxK

U2 - 10.1016/S1074-5521(98)90616-0

DO - 10.1016/S1074-5521(98)90616-0

M3 - Review article

C2 - 9578637

AN - SCOPUS:0031808658

SN - 1074-5521

VL - 5

SP - R105-R113

JO - Chemistry and Biology

JF - Chemistry and Biology

IS - 5

ER -

Stretching exercises - Flexibility in dihydrofolate reductase catalysis

Abstract

All Science Journal Classification (ASJC) codes

Access to Document

Other files and links

Fingerprint

Cite this