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rdf:type |
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lifeskim:mentions |
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pubmed:dateCreated |
1999-9-8
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pubmed:abstractText |
Vitamin K-dependent proteins contain a propeptide that is required for recognition by the enzyme gamma-glutamylcarboxylase. Substrates used in vitro for carboxylation studies lacking a prosequence are characterized by Km values in the millimolar range, whereas the Km for peptides containing a prosequence is three or four orders of magnitude smaller. Here we report that descarboxy-osteocalcin is an exception in this respect. With descarboxy-osteocalcin in purified propeptide-free recombinant carboxylase, the Km was 1.8 microM. Furthermore, osteocalcin was an inhibitor of descarboxy-osteocalcin carboxylation with a Ki of 76 microM. In contrast with the other vitamin K-dependent proteins, free propeptides do not inhibit descarboxy-osteocalcin carboxylation. Moreover, propeptide-containing substrates were inhibited neither by osteocalcin nor by its propeptide. From our studies we conclude that descarboxy-osteocalcin must have an internal recognition sequence that binds to gamma-glutamylcarboxylase at a site different from the propeptide-recognition site.
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/10393081-10068650,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10393081-1455398,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10393081-1499220,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10393081-1965174,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10393081-2006163,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10393081-2049381,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10393081-2183788,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10393081-2186178,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10393081-2198285,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10393081-2447082,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10393081-2664828,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10393081-2802629,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10393081-2890628,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10393081-3042764,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10393081-3060178,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10393081-3133366,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10393081-319462,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10393081-3499140,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10393081-3530902,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10393081-3802193,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10393081-3877721,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10393081-4040397,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10393081-426799,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10393081-7626624,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10393081-9052783,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10393081-9063025,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10393081-9163328,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10393081-9198222,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10393081-9330300
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Jul
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pubmed:issn |
0264-6021
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
15
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pubmed:volume |
341 ( Pt 2)
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
265-9
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pubmed:dateRevised |
2009-11-18
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pubmed:meshHeading |
pubmed-meshheading:10393081-Amino Acid Sequence,
pubmed-meshheading:10393081-Animals,
pubmed-meshheading:10393081-Binding Sites,
pubmed-meshheading:10393081-Carbon-Carbon Ligases,
pubmed-meshheading:10393081-Cell Line,
pubmed-meshheading:10393081-Molecular Sequence Data,
pubmed-meshheading:10393081-Osteocalcin,
pubmed-meshheading:10393081-Peptides,
pubmed-meshheading:10393081-Protein Binding,
pubmed-meshheading:10393081-Substrate Specificity,
pubmed-meshheading:10393081-Vitamin K
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pubmed:year |
1999
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pubmed:articleTitle |
Osteocalcin binds tightly to the gamma-glutamylcarboxylase at a site distinct from that of the other known vitamin K-dependent proteins.
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pubmed:affiliation |
Department of Biochemistry and Cardiovascular Research Institute, Maastricht University, P.O. Box 616, 6200 MD, Maastricht, The Netherlands.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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