The transformylase enzymes in de novo purine biosynthesis

Stephen J. Benkovic

doi:10.1016/0968-0004(84)90302-5

The transformylase enzymes in de novo purine biosynthesis

Stephen J. Benkovic

Chemistry

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

27 Scopus citations

Abstract

The two transformylase enzymes in de novo purine biosynthesis require 10-formyl-H₄folate as a cofactor, but can utilize efficiently differing synthetic analogs allowing their selective assay or inhibition. They, with a multifunctional enzyme responsible for cofactor synthesis, constitute a unique and possibly interacting subset within the de novo pathway.

Original language	English (US)
Pages (from-to)	320-322
Number of pages	3
Journal	Trends in Biochemical Sciences
Volume	9
Issue number	7
DOIs	https://doi.org/10.1016/0968-0004(84)90302-5
State	Published - Jul 1984

All Science Journal Classification (ASJC) codes

Biochemistry
Molecular Biology

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10.1016/0968-0004(84)90302-5

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title = "The transformylase enzymes in de novo purine biosynthesis",

abstract = "The two transformylase enzymes in de novo purine biosynthesis require 10-formyl-H4folate as a cofactor, but can utilize efficiently differing synthetic analogs allowing their selective assay or inhibition. They, with a multifunctional enzyme responsible for cofactor synthesis, constitute a unique and possibly interacting subset within the de novo pathway.",

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AU - Benkovic, Stephen J.

PY - 1984/7

Y1 - 1984/7

N2 - The two transformylase enzymes in de novo purine biosynthesis require 10-formyl-H4folate as a cofactor, but can utilize efficiently differing synthetic analogs allowing their selective assay or inhibition. They, with a multifunctional enzyme responsible for cofactor synthesis, constitute a unique and possibly interacting subset within the de novo pathway.

AB - The two transformylase enzymes in de novo purine biosynthesis require 10-formyl-H4folate as a cofactor, but can utilize efficiently differing synthetic analogs allowing their selective assay or inhibition. They, with a multifunctional enzyme responsible for cofactor synthesis, constitute a unique and possibly interacting subset within the de novo pathway.

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UR - https://www.scopus.com/pages/publications/0021191356#tab=citedBy

U2 - 10.1016/0968-0004(84)90302-5

DO - 10.1016/0968-0004(84)90302-5

M3 - Review article

AN - SCOPUS:0021191356

SN - 0968-0004

VL - 9

SP - 320

EP - 322

JO - Trends in Biochemical Sciences

JF - Trends in Biochemical Sciences

IS - 7

ER -

The transformylase enzymes in de novo purine biosynthesis

Abstract

All Science Journal Classification (ASJC) codes

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