Linked Life Data

681336

Source:http://linkedlifedata.com/resource/pubmed/id/681336

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
17
pubmed:dateCreated
1978-10-27
pubmed:abstractText
The arginine deiminase (L-arginine iminohydrolase, EC 3.5.3.6) from Mycoplasma arthritidis catalyzes the irreversible hydrolysis of arginine and related guanidine derivatives to ammonia and the corresponding ureido analog of the substrate. The kinetic constants Km, kcat, and kcat/Km for the arginine deiminase-catalyzed hydrolysis of L-arginine are equal to 4 micron, 29 s-1, and 7.4 X 10(7) M-1 s-1, respectively, at 25 degrees C and pH 7.2. The enzyme also catalyzes the hydrolysis of L-canavanine, Nalpha-methyl-L-argine, D-arginine, L-homoarginine, L-argininic acid, and guanidine, in order of decreasing second order rate constants (kcat/Km); the second order rate constants for these substrates are 10(-3) to 10(-10) smaller than the rate constant for L-arginine. Twenty-two arginine and guanidine analogs were tested for inhibitory capacity. Only 13 are competitive inhibitors having Ki values in the range 3.2 to 40 mM. These results show that binding of ligands to the enzyme is dominated by electrostatic or hydrogen bonding interactions, or both, of the guanidino and alpha-amino group. Neither citrulline nor ornithine, the end product of arginine degradation in M. arthritidis, is an inhibitor of arginine deiminase from this organism.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Sep
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
10
pubmed:volume
253
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
6016-20
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1978
pubmed:articleTitle
Arginine deiminase from Mycoplasma arthritidis. Structure-activity relationships among substrates and competitive inhibitors.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S.