Linked Life Data

6248027

Source:http://linkedlifedata.com/resource/pubmed/id/6248027

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
1980-8-15
pubmed:abstractText
1. The nature of arginine binding to lobster arginine kinase and the extent of its possible involvement with the ;essential' thiol group of the enzyme has been investigated with some inhibitory analogues of arginine. 2. Most of the analogues inhibit competitively, although mixed inhibition may occur if the alpha-carboxy group or alpha-amino group is absent. 3. The K(i) values indicate that strength of binding depends on the length of the carbon chain (l-isoleucine>l-valine>l- alpha-aminobutyrate>l-alanine) and the integrity of the substituents on the alpha-carbon atom (l-arginine>agmatine and l-ornithine>putrescine). The guanidino group probably contributes little to substrate binding, but a positive charge near the delta-nitrogen atom appears to be important (l-ornithine>l -citrulline>l-alpha-aminobutyrate). A cyclic analogue, 2-carboxymethyl-3-oxo-2,3,5,6,7,8-hexahydro-1H-imidazo [1,2-a][1,3]diazepine-8-carboxylic acid, has a low K(i) value similar to that of an equivalent straight-chain form, suggesting that arginine probably binds in a folded configuration. 4. The aliphatic l-amino acids give enzyme difference spectra similar to that with l-arginine and the integrity of the alpha-carboxy and alpha-amino groups appears to be a minimal but not sufficient requirement for this, as l-ornithine gives an atypical difference spectrum. A difference spectrum is interpreted as indicating an enzyme conformational change. No difference spectrum was observed with methylguanidine. 5. The ability of aliphatic alpha-l-amino acids to protect against inhibition by 5,5'-dithiobis-(2-nitrobenzoic acid) is proportional to the number of atoms in the carbon chain and inversely proportional to K(i). Ornithine gives greater protection than citrulline; analogues lacking the alpha-amino groups also protect. Agmatine, lacking the alpha-carboxy group, did not protect. 6. It is concluded that it is unlikely that the ;essential' thiol group in the enzyme interacts with any part of the arginine molecule during catalysis except, possibly, the alpha-carboxyl group.
pubmed:commentsCorrections
http://linkedlifedata.com/resource/pubmed/commentcorrection/6248027-13999246, http://linkedlifedata.com/resource/pubmed/commentcorrection/6248027-14232222, http://linkedlifedata.com/resource/pubmed/commentcorrection/6248027-170913, http://linkedlifedata.com/resource/pubmed/commentcorrection/6248027-171123, http://linkedlifedata.com/resource/pubmed/commentcorrection/6248027-182135, http://linkedlifedata.com/resource/pubmed/commentcorrection/6248027-4206907, http://linkedlifedata.com/resource/pubmed/commentcorrection/6248027-4797165, http://linkedlifedata.com/resource/pubmed/commentcorrection/6248027-4916855, http://linkedlifedata.com/resource/pubmed/commentcorrection/6248027-5075233, http://linkedlifedata.com/resource/pubmed/commentcorrection/6248027-5165680, http://linkedlifedata.com/resource/pubmed/commentcorrection/6248027-5459548, http://linkedlifedata.com/resource/pubmed/commentcorrection/6248027-5563365, http://linkedlifedata.com/resource/pubmed/commentcorrection/6248027-5729948, http://linkedlifedata.com/resource/pubmed/commentcorrection/6248027-5773441, http://linkedlifedata.com/resource/pubmed/commentcorrection/6248027-5965334
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Mar
pubmed:issn
0264-6021
pubmed:author
pubmed:issnType
Print
pubmed:day
1
pubmed:volume
185
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
593-9
pubmed:dateRevised
2009-11-18
pubmed:meshHeading
pubmed:year
1980
pubmed:articleTitle
The use of arginine analogues for investigating the functional organization of the arginine-binding site in lobster muscle arginine kinase. Role of the 'essential' thiol group.
pubmed:publicationType
Journal Article