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Journal article

Structure and mechanism of human UDP-xylose synthase: evidence for a promoting role of sugar ring distortion in a three-step catalytic conversion of UDP-glucuronic acid.

Abstract:

UDP-xylose synthase (UXS) catalyzes decarboxylation of UDP-D-glucuronic acid to UDP-xylose. In mammals, UDP-xylose serves to initiate glycosaminoglycan synthesis on the protein core of extracellular matrix proteoglycans. Lack of UXS activity leads to a defective extracellular matrix, resulting in strong interference with cell signaling pathways. We present comprehensive structural and mechanistic characterization of the human form of UXS. The 1.26-Å crystal structure of the enzyme bound with ...

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Publication status:
Published

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Publisher copy:
10.1074/jbc.m112.386706

Authors


Eixelsberger, T More by this author
Brunsteiner, M More by this author
Kavanagh, KL More by this author
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Journal:
The Journal of biological chemistry
Volume:
287
Issue:
37
Pages:
31349-31358
Publication date:
2012-09-05
DOI:
EISSN:
1083-351X
ISSN:
0021-9258
URN:
uuid:b0240334-c657-4774-99df-8b28f0e39456
Source identifiers:
342330
Local pid:
pubs:342330

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