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Title		Authors	PubMed ID
1	The binding of Na(+) to apo-enolase permits the binding of substrate.	Lin T, Kornblatt MJ	10669792 CHEMBIOCHEM
2	Cloning, expression and mutagenesis of a subunit contact of rabbit muscle-specific (betabeta) enolase.	Kornblatt MJ, Zheng SX, Lamandé N, Lazar M	12044909 CHEMBIOCHEM
3	The Energetics of Streptococcal Enolase Octamer Formation: The Quantitative Contributions of the Last Eight Amino Acids at the Carboxy-Terminus.	Kornblatt JA, Quiros V, Kornblatt MJ	26287818 BIOLOGY
4	Altering Residue 134 Confers an Increased Substrate Range of Alkylated Nucleosides to the E. coli OGT Protein.	Schoonhoven NM, O'Flaherty DK, McManus FP, Sacre L, Noronha AM, Kornblatt MJ, Wilds CJ	29137116 CHEMBIOCHEM
5	The influence of truncating the carboxy-terminal amino acid residues of streptococcal enolase on its ability to interact with canine plasminogen.	Deshmukh SS, Kornblatt MJ, Kornblatt JA	30653526 BIOLOGY

Title:	The binding of Na(+) to apo-enolase permits the binding of substrate.
Authors:	Lin T, Kornblatt MJ
Link:	https://www.ncbi.nlm.nih.gov/pubmed/10669792?dopt=Abstract
DOI:	10.1016/s0167-4838(99)00233-2
Publication:	Biochimica et biophysica acta
Keywords:
PMID:	10669792	Category:	Biochim Biophys Acta	Date Added:	2019-06-20
Dept Affiliation:	CHEMBIOCHEM 1 Enzyme Research Group, Department of Chemistry and Biochemistry, Concordia University, 1455 de Maisonneuve Boulevard W., Montreal, Que., Canada.

Description:

The binding of Na(+) to apo-enolase permits the binding of substrate.

Biochim Biophys Acta. 2000 Feb 09;1476(2):279-86

Authors: Lin T, Kornblatt MJ

Abstract

Enolase from rabbit muscle (betabeta-enolase) is inactivated by NaClO(4). Enolase free of divalent cations is more susceptible to inactivation by NaClO(4) than is enolase in the presence of Mg(2+). We find that substrate protects apo-enolase against inactivation, indicating that substrate can bind to enolase in the absence of a divalent cation. This binding is not due to contamination by trace levels of divalent cations since (1) it occurs even in the presence of EDTA or EGTA and (2) metal analysis by ICP (inductively coupled plasma) mass spectrometry did not reveal sufficient contamination to account for the protection. The binding of PGA to apo-enolase did require Na(+). When TMAClO(4) was used instead of NaClO(4), there was no protection by PGA. Protection was restored when TMAClO(4) plus NaCl were used. The inactivation of apo-enolase by NaClO(4) is due to dissociation into inactive monomers. We conclude that Na(+) binds to apo-enolase, permitting substrate to then bind. Of the three known Me(2+) binding sites on enolase, we believe the most likely binding site for Na(+) is the carboxylate cluster of site 1, the highest affinity site of enolase.

PMID: 10669792 [PubMed - indexed for MEDLINE]

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