Hypoxia-inducible factor asparaginyl hydroxylase (FIH-1) catalyses hydroxylation at the beta-carbon of asparagine-803

L A  McNeill; K S  Hewitson; T D  Claridge; J F  Seibel; L E  Horsfall; C J  Schofield

doi:10.1042/BJ20021162

Hypoxia-inducible factor asparaginyl hydroxylase (FIH-1) catalyses hydroxylation at the beta-carbon of asparagine-803

L A McNeill, K S Hewitson, T D Claridge, J F Seibel, L E Horsfall, C J Schofield

School of Biological Sciences

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

Abstract / Description of output

Asparagine-803 in the C-terminal transactivation domain of human hypoxia-inducible factor (HIF)-1 alpha-subunit is hydroxylated by factor inhibiting HIF-1 (FIH-1) under normoxic conditions causing abrogation of the HIF-1alpha/p300 interaction. NMR and other analyses of a hydroxylated HIF fragment produced in vitro demonstrate that hydroxylation occurs at the beta-carbon of Asn-803 and imply production of the threo-isomer, in contrast with other known aspartic acid/asparagine hydroxylases that produce the erythro-isomer.

Original language	English
Pages (from-to)	571-575
Number of pages	5
Journal	Biochemical Journal
Volume	367
DOIs	https://doi.org/10.1042/BJ20021162
Publication status	Published - 1 Nov 2002

Keywords / Materials (for Non-textual outputs)

asparagine hydroxylation
factor inhibiting hypoxia-inducible factor-1 (FIH-1)
hypoxia
oxygenase
oxygen sensing

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10.1042/BJ20021162

http://www.ncbi.nlm.nih.gov/pmc/articles/PMC1222951/pdf/12215170.pdf

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@article{155bbc09d47d4e41957127a2089d2922,

title = "Hypoxia-inducible factor asparaginyl hydroxylase (FIH-1) catalyses hydroxylation at the beta-carbon of asparagine-803",

abstract = "Asparagine-803 in the C-terminal transactivation domain of human hypoxia-inducible factor (HIF)-1 alpha-subunit is hydroxylated by factor inhibiting HIF-1 (FIH-1) under normoxic conditions causing abrogation of the HIF-1alpha/p300 interaction. NMR and other analyses of a hydroxylated HIF fragment produced in vitro demonstrate that hydroxylation occurs at the beta-carbon of Asn-803 and imply production of the threo-isomer, in contrast with other known aspartic acid/asparagine hydroxylases that produce the erythro-isomer.",

keywords = "asparagine hydroxylation, factor inhibiting hypoxia-inducible factor-1 (FIH-1), hypoxia, oxygenase, oxygen sensing",

author = "McNeill, {L A} and Hewitson, {K S} and Claridge, {T D} and Seibel, {J F} and Horsfall, {L E} and Schofield, {C J}",

year = "2002",

month = nov,

day = "1",

doi = "10.1042/BJ20021162",

language = "English",

volume = "367",

pages = "571--575",

journal = "Biochemical Journal",

issn = "0264-6021",

publisher = "Portland Press Ltd.",

}

TY - JOUR

T1 - Hypoxia-inducible factor asparaginyl hydroxylase (FIH-1) catalyses hydroxylation at the beta-carbon of asparagine-803

AU - McNeill, L A

AU - Hewitson, K S

AU - Claridge, T D

AU - Seibel, J F

AU - Horsfall, L E

AU - Schofield, C J

PY - 2002/11/1

Y1 - 2002/11/1

N2 - Asparagine-803 in the C-terminal transactivation domain of human hypoxia-inducible factor (HIF)-1 alpha-subunit is hydroxylated by factor inhibiting HIF-1 (FIH-1) under normoxic conditions causing abrogation of the HIF-1alpha/p300 interaction. NMR and other analyses of a hydroxylated HIF fragment produced in vitro demonstrate that hydroxylation occurs at the beta-carbon of Asn-803 and imply production of the threo-isomer, in contrast with other known aspartic acid/asparagine hydroxylases that produce the erythro-isomer.

AB - Asparagine-803 in the C-terminal transactivation domain of human hypoxia-inducible factor (HIF)-1 alpha-subunit is hydroxylated by factor inhibiting HIF-1 (FIH-1) under normoxic conditions causing abrogation of the HIF-1alpha/p300 interaction. NMR and other analyses of a hydroxylated HIF fragment produced in vitro demonstrate that hydroxylation occurs at the beta-carbon of Asn-803 and imply production of the threo-isomer, in contrast with other known aspartic acid/asparagine hydroxylases that produce the erythro-isomer.

KW - asparagine hydroxylation

KW - factor inhibiting hypoxia-inducible factor-1 (FIH-1)

KW - hypoxia

KW - oxygenase

KW - oxygen sensing

U2 - 10.1042/BJ20021162

DO - 10.1042/BJ20021162

M3 - Article

SN - 0264-6021

VL - 367

SP - 571

EP - 575

JO - Biochemical Journal

JF - Biochemical Journal

ER -

Hypoxia-inducible factor asparaginyl hydroxylase (FIH-1) catalyses hydroxylation at the beta-carbon of asparagine-803

Abstract / Description of output

Keywords / Materials (for Non-textual outputs)

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