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Novel role of tyrosine in catalysis by human AP endonuclease 1.

Abstract：

:Apurinic/apyrimidinic endonuclease (AP endo, HAP1) recognizes abasic sites in ds DNA and makes a single nick in the backbone 5' to the abasic site. In this report we examine the roles of three conserved tyrosine residues in close proximity to the active site. We show that Tyr(128) and Tyr(269), which interact upstream and downstream of the abasic site, respectively, are involved in recognition and binding of abasic site-containing double stranded DNA. However, the two residues are not equivalent, as their effects are differentiated by changes in salt concentration. In sharp contrast, Tyr(171) is directly involved in catalysis as well as binding. Y171F, Y171H, and Y171A all show decreased catalytic efficiencies 25,000-50,000-fold from the WT enzyme. Both imidazole and basic pH markedly stimulate the WT enzyme. Imidazole stimulates Tyr(171) mutant enzymes when tyrosine is also present but basic pH eliminates remaining mutant activity. These results underscore the importance of tyrosines in AP endo catalysis. They render the current hypotheses regarding enzyme action unlikely and allow us to consider the possibility that the phenolate of Tyr(171) is the nucleophile that attacks the scissile phosphate.

journal_name

DNA Repair (Amst)

journal_title

DNA repair

authors

Mundle ST,Fattal MH,Melo LF,Coriolan JD,O'Regan NE,Strauss PR

doi

10.1016/j.dnarep.2004.06.009

keywords:

subject

Has Abstract

pub_date

2004-11-02 00:00:00

pages

1447-55

issue

11

eissn

1568-7864

issn

1568-7856

pii

S1568-7864(04)00185-5

journal_volume

3

pub_type

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