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Mg-phosphonoacetohydroxamate complex of S39A yeast enolase 1
Descriptor:	MAGNESIUM ION, PHOSPHONOACETOHYDROXAMIC ACID, enolase 1
Authors:	Poyner, R.R, Larsen, T.M, Wong, S.W, Reed, G.H.
Deposit date:	2002-03-21
Release date:	2002-04-03
Last modified:	2024-02-14
Method:	X-RAY DIFFRACTION (2.1 Å)
Cite:	Functional and structural changes due to a serine to alanine mutation in the active-site flap of enolase. Arch.Biochem.Biophys., 401, 2002

REVERSE PROTONATION IS THE KEY TO GENERAL ACID-BASE CATALYSIS IN ENOLASE
Descriptor:	2-PHOSPHOGLYCERIC ACID, Enolase 1, MAGNESIUM ION
Authors:	Sims, P.A, Larsen, T.M, Poyner, R.R, Cleland, W.W, Reed, G.H.
Deposit date:	2003-04-21
Release date:	2003-11-18
Last modified:	2024-02-14
Method:	X-RAY DIFFRACTION (1.8 Å)
Cite:	Reverse protonation is the key to general acid-base catalysis in enolase Biochemistry, 42, 2003

REVERSE PROTONATION IS THE KEY TO GENERAL ACID-BASE CATALYSIS IN ENOLASE
Descriptor:	Enolase 1, MAGNESIUM ION, PHOSPHOENOLPYRUVATE
Authors:	Sims, P.A, Larsen, T.M, Poyner, R.R, Cleland, W.W, Reed, G.H.
Deposit date:	2003-04-21
Release date:	2003-11-18
Last modified:	2024-02-14
Method:	X-RAY DIFFRACTION (2 Å)
Cite:	Reverse protonation is the key to general acid-base catalysis in enolase Biochemistry, 42, 2003

CHELATION OF SER 39 TO MG2+ LATCHES A GATE AT THE ACTIVE SITE OF ENOLASE: STRUCTURE OF THE BIS(MG2+) COMPLEX OF YEAST ENOLASE AND THE INTERMEDIATE ANALOG PHOSPHONOACETOHYDROXAMATE AT 2.1 ANGSTROMS RESOLUTION
Descriptor:	ENOLASE, MAGNESIUM ION, PHOSPHONOACETOHYDROXAMIC ACID
Authors:	Wedekind, J.E, Reed, G.H, Rayment, I.
Deposit date:	1994-04-27
Release date:	1995-04-27
Last modified:	2024-02-07
Method:	X-RAY DIFFRACTION (2.1 Å)
Cite:	Chelation of serine 39 to Mg2+ latches a gate at the active site of enolase: structure of the bis(Mg2+) complex of yeast enolase and the intermediate analog phosphonoacetohydroxamate at 2.1-A resolution. Biochemistry, 33, 1994