Adenylate deaminase: Potent inhibition by 2′-deoxycoformycin 5′-phosphate

Carl Frieden; Helen R. Gilbert; Wayne H. Miller; Richard L. Miller

doi:10.1016/0006-291X(79)90614-4

Adenylate deaminase: Potent inhibition by 2′-deoxycoformycin 5′-phosphate

Carl Frieden
, Helen R. Gilbert
, Wayne H. Miller
, Richard L. Miller

Research output: Contribution to journal › Article › peer-review

20 Scopus citations

Abstract

The nucleotide 2′-deoxycoformycin 5′-phosphate has been enzymatically synthesized from 2′-deoxycoformycin and found to be a potent stoichiometric inhibitor of adenylate deaminase from rabbit muscle. It is shown that the inhibitor binds to the active site and may be considered as a possible transition state analog. The inhibition is time dependent which may reflect an inhibitor induced conformational change.

Original language	English
Pages (from-to)	278-283
Number of pages	6
Journal	Biochemical and Biophysical Research Communications
Volume	91
Issue number	1
DOIs	https://doi.org/10.1016/0006-291X(79)90614-4
State	Published - Nov 14 1979

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title = "Adenylate deaminase: Potent inhibition by 2′-deoxycoformycin 5′-phosphate",

abstract = "The nucleotide 2′-deoxycoformycin 5′-phosphate has been enzymatically synthesized from 2′-deoxycoformycin and found to be a potent stoichiometric inhibitor of adenylate deaminase from rabbit muscle. It is shown that the inhibitor binds to the active site and may be considered as a possible transition state analog. The inhibition is time dependent which may reflect an inhibitor induced conformational change.",

author = "Carl Frieden and Gilbert, \{Helen R.\} and Miller, \{Wayne H.\} and Miller, \{Richard L.\}",

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T2 - Potent inhibition by 2′-deoxycoformycin 5′-phosphate

AU - Frieden, Carl

AU - Gilbert, Helen R.

AU - Miller, Wayne H.

AU - Miller, Richard L.

PY - 1979/11/14

Y1 - 1979/11/14

N2 - The nucleotide 2′-deoxycoformycin 5′-phosphate has been enzymatically synthesized from 2′-deoxycoformycin and found to be a potent stoichiometric inhibitor of adenylate deaminase from rabbit muscle. It is shown that the inhibitor binds to the active site and may be considered as a possible transition state analog. The inhibition is time dependent which may reflect an inhibitor induced conformational change.

AB - The nucleotide 2′-deoxycoformycin 5′-phosphate has been enzymatically synthesized from 2′-deoxycoformycin and found to be a potent stoichiometric inhibitor of adenylate deaminase from rabbit muscle. It is shown that the inhibitor binds to the active site and may be considered as a possible transition state analog. The inhibition is time dependent which may reflect an inhibitor induced conformational change.

UR - https://www.scopus.com/pages/publications/0018594339

U2 - 10.1016/0006-291X(79)90614-4

DO - 10.1016/0006-291X(79)90614-4

M3 - Article

C2 - 518627

AN - SCOPUS:0018594339

SN - 0006-291X

VL - 91

SP - 278

EP - 283

JO - Biochemical and Biophysical Research Communications

JF - Biochemical and Biophysical Research Communications

IS - 1

ER -

Adenylate deaminase: Potent inhibition by 2′-deoxycoformycin 5′-phosphate

Abstract

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