Pre-Steady-State Reactivity of Peptidylglycine Monooxygenase Implicates Ascorbate in Substrate Triggering of the Active Conformer-Reference-Cited by-同舟云学术

Pre-Steady-State Reactivity of Peptidylglycine Monooxygenase Implicates Ascorbate in Substrate Triggering of the Active Conformer

Published:2022-04-05 Issue:8 Volume:61 Page:665-677
ISSN:0006-2960
Container-title:Biochemistry
language:en
Short-container-title:Biochemistry

Author:

Welch Evan F.¹²,Rush Katherine W.¹³^ORCID,Arias Renee J.¹^ORCID,Blackburn Ninian J.¹^ORCID

Affiliation:

1. Department of Chemical Physiology and Biochemistry, Oregon Health and Science University, 3181 SW Sam Jackson Park Road, Portland, Oregon 97239, United States

2. Department of Biomedical Engineering, Oregon Health and Science University, 3181 SW Sam Jackson Park Road, Portland, Oregon 97239, United States

3. Department of Chemistry, Reed College, 3203 SE Woodstock Blvd, Portland, Oregon 97202, United States

Funder

National Institute of General Medical Sciences

Publisher

American Chemical Society (ACS)

Subject

Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/acs.biochem.2c00080

Reference53 articles.

1. The Copper-Enzyme Family of Dopamine β-Monooxygenase and Peptidylglycine α-Hydroxylating Monooxygenase: Resolving the Chemical Pathway for Substrate Hydroxylation

2. The crystal structure of human dopamine β-hydroxylase at 2.9 Å resolution

3. The copper centers of tyramine β-monooxygenase and its catalytic-site methionine variants: an X-ray absorption study

4. New insights into copper monooxygenases and peptide amidation: structure, mechanism and function

5. 60 YEARS OF POMC: From POMC and α-MSH to PAM, molecular oxygen, copper, and vitamin C

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4. New structures reveal flexible dynamics between the subdomains of peptidylglycine monooxygenase. Implications for an open to closed mechanism;Protein Science;2023-03-22