Abstract
At least one arginine residue is essential for substrate binding in or near the active sites of propionyl CoA carboxylase (PCC) and beta-methylcrotonyl CoA carboxylase (beta MCC) in cultured human fibroblasts. This conclusion is based on studies of enzyme inhibition by phenylglyoxal, a reagent which specifically modifies arginine residues. Human fibroblast PCC both in extracts and in a 20-fold purified preparation was nearly completely protected from phenylglyoxal inhibition following incubation with propionyl CoA or ATP. It appears that a phosphate group from either ATP or the CoA moiety of propionyl CoA reacts with the essential arginine residue(s). beta MCC which was similarly inhibited by phenylglyoxal was protected by beta-methylcrotonyl CoA and ATP. Thus phenylglyoxal may be used to label specific arginine residues within the active sites of previously sequenced carboxylases.
| Original language | English (US) |
|---|---|
| Pages (from-to) | 302-306 |
| Number of pages | 5 |
| Journal | Enzyme |
| Volume | 24 |
| Issue number | 5 |
| DOIs | |
| State | Published - Jan 1 1979 |
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ASJC Scopus subject areas
- Biochemistry
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Essential arginine residues in the active sites of propionyl CoA carboxylase and beta-methylcrotonyl CoA carboxylase. / Wolf, B.; Kalousek, F.; Rosenberg, L. E.
In: Enzyme, Vol. 24, No. 5, 01.01.1979, p. 302-306.Research output: Contribution to journal › Article
TY - JOUR
T1 - Essential arginine residues in the active sites of propionyl CoA carboxylase and beta-methylcrotonyl CoA carboxylase.
AU - Wolf, B.
AU - Kalousek, F.
AU - Rosenberg, L. E.
PY - 1979/1/1
Y1 - 1979/1/1
N2 - At least one arginine residue is essential for substrate binding in or near the active sites of propionyl CoA carboxylase (PCC) and beta-methylcrotonyl CoA carboxylase (beta MCC) in cultured human fibroblasts. This conclusion is based on studies of enzyme inhibition by phenylglyoxal, a reagent which specifically modifies arginine residues. Human fibroblast PCC both in extracts and in a 20-fold purified preparation was nearly completely protected from phenylglyoxal inhibition following incubation with propionyl CoA or ATP. It appears that a phosphate group from either ATP or the CoA moiety of propionyl CoA reacts with the essential arginine residue(s). beta MCC which was similarly inhibited by phenylglyoxal was protected by beta-methylcrotonyl CoA and ATP. Thus phenylglyoxal may be used to label specific arginine residues within the active sites of previously sequenced carboxylases.
AB - At least one arginine residue is essential for substrate binding in or near the active sites of propionyl CoA carboxylase (PCC) and beta-methylcrotonyl CoA carboxylase (beta MCC) in cultured human fibroblasts. This conclusion is based on studies of enzyme inhibition by phenylglyoxal, a reagent which specifically modifies arginine residues. Human fibroblast PCC both in extracts and in a 20-fold purified preparation was nearly completely protected from phenylglyoxal inhibition following incubation with propionyl CoA or ATP. It appears that a phosphate group from either ATP or the CoA moiety of propionyl CoA reacts with the essential arginine residue(s). beta MCC which was similarly inhibited by phenylglyoxal was protected by beta-methylcrotonyl CoA and ATP. Thus phenylglyoxal may be used to label specific arginine residues within the active sites of previously sequenced carboxylases.
UR - http://www.scopus.com/inward/record.url?scp=0018628966&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0018628966&partnerID=8YFLogxK
U2 - 10.1159/000458679
DO - 10.1159/000458679
M3 - Article
C2 - 510274
AN - SCOPUS:0018628966
VL - 24
SP - 302
EP - 306
JO - Enzyme
JF - Enzyme
SN - 0013-9432
IS - 5
ER -