Abstract:
:Gellan gum is a widely used commercial material, available in many different forms. Its economic importance has led to studies into the biosynthesis of exopolysaccharide gellan gum, which is industrially prepared in high yields using Sphingomonas elodea ATCC 31461. Glucose-1-phosphate uridylyltransferase mediates the reversible conversion of glucose-1-phosphate and UTP into UDP-glucose and pyrophosphate, which is a key step in the biosynthetic pathway of gellan gums. Here we present the X-ray crystal structure of the glucose-1-phosphate uridylyltransferase from S. elodea. The S. elodea enzyme shares strong monomeric similarity with glucose-1-phosphate thymidylyltransferase, several structures of which are known, although the quaternary structures of the active enzymes are rather different. A detailed comparison between S. elodea glucose-1-phosphate uridylyltransferase and available thymidylyltransferases is described and shows remarkable structural similarities, despite the low sequence identities between the two divergent groups of proteins.
journal_name
J Bacterioljournal_title
Journal of bacteriologyauthors
Aragão D,Fialho AM,Marques AR,Mitchell EP,Sá-Correia I,Frazão Cdoi
10.1128/JB.00277-07subject
Has Abstractpub_date
2007-06-01 00:00:00pages
4520-8issue
12eissn
0021-9193issn
1098-5530pii
JB.00277-07journal_volume
189pub_type
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journal_title:Journal of bacteriology
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journal_title:Journal of bacteriology
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pub_type: 杂志文章
doi:10.1128/jb.171.2.643-649.1989
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pub_type: 杂志文章
doi:10.1128/JB.103.1.9-15.1970
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journal_title:Journal of bacteriology
pub_type: 杂志文章
doi:10.1128/JB.161.2.696-701.1985
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journal_title:Journal of bacteriology
pub_type: 杂志文章
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journal_title:Journal of bacteriology
pub_type: 杂志文章
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更新日期:1991-08-01 00:00:00