X-ray crystallographic determination of the structure of bovine lens leucine aminopeptidase complexed with amastatin: Formulation of a catalytic mechanism featuring a gem-diolate transition state

Hidong Kim; William N. Lipscomb

doi:10.1021/bi00084a011

X-ray crystallographic determination of the structure of bovine lens leucine aminopeptidase complexed with amastatin: Formulation of a catalytic mechanism featuring a gem-diolate transition state

Biochemistry ◽

10.1021/bi00084a011 ◽

1993 ◽

Vol 32 (33) ◽

pp. 8465-8478 ◽

Cited By ~ 78

Author(s):

Hidong Kim ◽

William N. Lipscomb

Keyword(s):

Transition State ◽

Catalytic Mechanism ◽

Leucine Aminopeptidase ◽

X Ray ◽

Bovine Lens

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Transition State Analog L-Leucinephosphonic Acid Bound to Bovine Lens Leucine Aminopeptidase: X-ray Structure at 1.65 .ANG. Resolution in a New Crystal Form

Biochemistry ◽

10.1021/bi00028a033 ◽

1995 ◽

Vol 34 (28) ◽

pp. 9200-9210 ◽

Cited By ~ 91

Author(s):

Norbert Strater ◽

William N. Lipscomb

Keyword(s):

Transition State ◽

Leucine Aminopeptidase ◽

Crystal Form ◽

Transition State Analog ◽

X Ray ◽

Bovine Lens

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Two-Metal Ion Mechanism of Bovine Lens Leucine Aminopeptidase: Active Site Solvent Structure and Binding Mode of L-Leucinal, a gem-Diolate Transition State Analog, by X-ray Crystallography

Biochemistry ◽

10.1021/bi00045a021 ◽

1995 ◽

Vol 34 (45) ◽

pp. 14792-14800 ◽

Cited By ~ 116

Author(s):

Norbert Straeter ◽

William N. Lipscomb

Keyword(s):

Transition State ◽

Active Site ◽

Metal Ion ◽

Leucine Aminopeptidase ◽

Binding Mode ◽

Solvent Structure ◽

Transition State Analog ◽

X Ray ◽

X Ray Crystallography ◽

Bovine Lens

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Leucine aminopeptidase from bovine lens and hog kidney. Comparison using immunological techniques, electron microscopy, and X-ray diffraction.

Journal of Biological Chemistry ◽

10.1016/s0021-9258(17)42667-6 ◽

1984 ◽

Vol 259 (23) ◽

pp. 14757-14761 ◽

Cited By ~ 5

Author(s):

A Taylor ◽

K W Volz ◽

W N Lipscomb ◽

L J Takemoto

Keyword(s):

Electron Microscopy ◽

Leucine Aminopeptidase ◽

X Ray Diffraction ◽

X Ray ◽

Bovine Lens ◽

Hog Kidney

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Differentiation and identification of the two catalytic metal binding sites in bovine lens leucine aminopeptidase by x-ray crystallography.

Proceedings of the National Academy of Sciences ◽

10.1073/pnas.90.11.5006 ◽

1993 ◽

Vol 90 (11) ◽

pp. 5006-5010 ◽

Cited By ~ 69

Author(s):

H. Kim ◽

W. N. Lipscomb

Keyword(s):

Metal Binding ◽

Binding Sites ◽

Leucine Aminopeptidase ◽

X Ray ◽

X Ray Crystallography ◽

Metal Binding Sites ◽

Bovine Lens ◽

Catalytic Metal

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Re-refinement of the X-ray Crystal Structure of Bovine Lens Leucine Aminopeptidase Complexed with Bestatin

Journal of Molecular Biology ◽

10.1006/jmbi.1993.1193 ◽

1993 ◽

Vol 230 (3) ◽

pp. 722-724 ◽

Cited By ~ 28

Author(s):

Hidong Kim ◽

Stephen K. Burley ◽

William N. Lipscomb

Keyword(s):

Crystal Structure ◽

Leucine Aminopeptidase ◽

X Ray ◽

Bovine Lens

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Determination of reaction intermediates and catalytic mechanism by X-ray diffraction

Acta Crystallographica Section A Foundations and Advances ◽

10.1107/s2053273317092786 ◽

2017 ◽

Vol 73 (a2) ◽

pp. C295-C295

Author(s):

Wei Yang

Keyword(s):

Catalytic Mechanism ◽

Reaction Intermediates ◽

X Ray Diffraction ◽

X Ray

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Preliminary X-ray study of leucine aminopeptidase (bovine lens), an oligomeric metalloenzyme

Journal of Molecular Biology ◽

10.1016/s0022-2836(77)80162-9 ◽

1977 ◽

Vol 112 (1) ◽

pp. 149-153 ◽

Cited By ~ 20

Author(s):

Frances Jurnak ◽

Alexander Rich ◽

Lucy van Loon-Klaassen ◽

Hans Bloemendal ◽

Allen Taylor ◽

...

Keyword(s):

Leucine Aminopeptidase ◽

X Ray ◽

Bovine Lens

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Catalytic Mechanism of the Hotdog-Fold Thioesterase PA1618 Revealed by X-ray Structure Determination of a Substrate-Bound Oxygen Ester Analogue Complex

ChemBioChem ◽

10.1002/cbic.201700322 ◽

2017 ◽

Vol 18 (19) ◽

pp. 1935-1943

Author(s):

John A. Latham ◽

Tianyang Ji ◽

Kaila Matthews ◽

Patrick S. Mariano ◽

Karen N. Allen ◽

...

Keyword(s):

Structure Determination ◽

Catalytic Mechanism ◽

X Ray ◽

Hotdog Fold

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Catalytic mechanism of the inverting N-acetylglucosaminyltransferase I: DFT quantum mechanical model of the reaction pathway and determination of the transition state structure

Glycobiology ◽

10.1093/glycob/cwg067 ◽

2003 ◽

Vol 13 (8) ◽

pp. 559-566 ◽

Cited By ~ 16

Author(s):

I. Tvaroska

Keyword(s):

Transition State ◽

Mechanical Model ◽

Catalytic Mechanism ◽

Reaction Pathway ◽

Quantum Mechanical ◽

State Structure ◽

Transition State Structure ◽

Quantum Mechanical Model

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Ab Initio Molecular Orbital Study of the Catalytic Mechanism of Glycosyltransferases: Description of Reaction Pathways and Determination of Transition-State Structures for InvertingN-Acetylglucosaminyltransferases

Journal of the American Chemical Society ◽

10.1021/ja001525u ◽

2000 ◽

Vol 122 (36) ◽

pp. 8762-8776 ◽

Cited By ~ 42

Author(s):

Igor Tvaroska ◽

Isabelle André ◽

Jeremy P. Carver

Keyword(s):

Transition State ◽

Ab Initio ◽

Molecular Orbital ◽

Catalytic Mechanism ◽

Reaction Pathways ◽

Molecular Orbital Study ◽

Orbital Study ◽

Transition State Structures

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