Structural Analysis of Mammalian Cytochrome P450 2B4 Covalently Bound to the Mechanism-Based Inactivator tert -Butylphenylacetylene: Insight into Partial Enzymatic Activity (Q27667508)

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English	Structural Analysis of Mammalian Cytochrome P450 2B4 Covalently Bound to the Mechanism-Based Inactivator tert -Butylphenylacetylene: Insight into Partial Enzymatic Activity	scientific article

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scholarly article

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Structural Analysis of Mammalian Cytochrome P450 2B4 Covalently Bound to the Mechanism-Based Inactivator tert -Butylphenylacetylene: Insight into Partial Enzymatic Activity (English)

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author name string

Sean C Gay

1

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Haoming Zhang

2

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P Ross Wilderman

3

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Arthur G Roberts

4

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Tong Liu

5

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Sheng Li

6

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Hsia-Lien Lin

7

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Qinghai Zhang

8

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Virgil L Woods

9

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C David Stout

10

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Paul F Hollenberg

11

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James R Halpert

12

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language of work or name

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publication date

7 June 2011

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50

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22

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4903-11

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The structure of CYP101D2 unveils a potential path for substrate entry into the active site

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Covalent modification of Thr302 in cytochrome P450 2B1 by the mechanism-based inactivator 4-tert-butylphenylacetylene

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1 reference

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1 reference

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1 reference

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1 reference

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1 reference

https://pubmed.ncbi.nlm.nih.gov/21510666

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inferred from PubMed ID database lookup

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1 reference

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1 reference

https://pubmed.ncbi.nlm.nih.gov/21510666

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Identifiers

10.1021/BI200482G

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