Mutant N143P Reveals How Na+ Activates Thrombin

The molecular mechanism of thrombin activation by Na+ remains elusive. Its kinetic formulation requires extension of the classical Botts-Morales theory for the action of a modifier on an enzyme to correctly account for the contribution of the E*, E, and E:Na+ forms. The extended scheme establishes t...

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Published inThe Journal of biological chemistry Vol. 284; no. 52; pp. 36175 - 36185
Main Authors Niu, Weiling, Chen, Zhiwei, Bush-Pelc, Leslie A., Bah, Alaji, Gandhi, Prafull S., Di Cera, Enrico
Format Journal Article
LanguageEnglish
Published United States Elsevier Inc 25.12.2009
American Society for Biochemistry and Molecular Biology
Subjects
AFFINITY
Allosteric Regulation - genetics
Amino Acid Substitution
ARCHITECTURE
ATOMS
CARBONYLS
CRYSTAL STRUCTURE
Crystallography, X-Ray
Enzyme Activation - genetics
Enzyme Catalysis and Regulation
ENZYMES
Humans
Hydrogen Bonding
KINETICS
MATERIALS SCIENCE
MUTANTS
Mutation, Missense
ORIENTATION
PEPTIDES
Protein Binding - genetics
Protein Structure, Tertiary - physiology
RESIDUES
Sodium - chemistry
Sodium - metabolism
Structure-Activity Relationship
THROMBIN
Thrombin - chemistry
Thrombin - genetics
Thrombin - metabolism
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Abstract The molecular mechanism of thrombin activation by Na+ remains elusive. Its kinetic formulation requires extension of the classical Botts-Morales theory for the action of a modifier on an enzyme to correctly account for the contribution of the E*, E, and E:Na+ forms. The extended scheme establishes that analysis of kcat unequivocally identifies allosteric transduction of Na+ binding into enhanced catalytic activity. The thrombin mutant N143P features no Na+-dependent enhancement of kcat yet binds Na+ with an affinity comparable to that of wild type. Crystal structures of the mutant in the presence and absence of Na+ confirm that Pro143 abrogates the important H-bond between the backbone N atom of residue 143 and the carbonyl O atom of Glu192, which in turn controls the orientation of the Glu192-Gly193 peptide bond and the correct architecture of the oxyanion hole. We conclude that Na+ activates thrombin by securing the correct orientation of the Glu192-Gly193 peptide bond, which is likely flipped in the absence of cation. Absolute conservation of the 143–192 H-bond in trypsin-like proteases and the importance of the oxyanion hole in protease function suggest that this mechanism of Na+ activation is present in all Na+-activated trypsin-like proteases.
AbstractList The molecular mechanism of thrombin activation by Na + remains elusive. Its kinetic formulation requires extension of the classical Botts-Morales theory for the action of a modifier on an enzyme to correctly account for the contribution of the E *, E , and E :Na + forms. The extended scheme establishes that analysis of k cat unequivocally identifies allosteric transduction of Na + binding into enhanced catalytic activity. The thrombin mutant N143P features no Na + -dependent enhancement of k cat yet binds Na + with an affinity comparable to that of wild type. Crystal structures of the mutant in the presence and absence of Na + confirm that Pro 143 abrogates the important H-bond between the backbone N atom of residue 143 and the carbonyl O atom of Glu 192 , which in turn controls the orientation of the Glu 192 -Gly 193 peptide bond and the correct architecture of the oxyanion hole. We conclude that Na + activates thrombin by securing the correct orientation of the Glu 192 -Gly 193 peptide bond, which is likely flipped in the absence of cation. Absolute conservation of the 143–192 H-bond in trypsin-like proteases and the importance of the oxyanion hole in protease function suggest that this mechanism of Na + activation is present in all Na + -activated trypsin-like proteases.
The molecular mechanism of thrombin activation by Na + remains elusive. Its kinetic formulation requires extension of the classical Botts-Morales theory for the action of a modifier on an enzyme to correctly account for the contribution of the E *, E , and E :Na + forms. The extended scheme establishes that analysis of k cat unequivocally identifies allosteric transduction of Na + binding into enhanced catalytic activity. The thrombin mutant N143P features no Na + -dependent enhancement of k cat yet binds Na + with an affinity comparable to that of wild type. Crystal structures of the mutant in the presence and absence of Na + confirm that Pro 143 abrogates the important H-bond between the backbone N atom of residue 143 and the carbonyl O atom of Glu 192 , which in turn controls the orientation of the Glu 192 -Gly 193 peptide bond and the correct architecture of the oxyanion hole. We conclude that Na + activates thrombin by securing the correct orientation of the Glu 192 -Gly 193 peptide bond, which is likely flipped in the absence of cation. Absolute conservation of the 143–192 H-bond in trypsin-like proteases and the importance of the oxyanion hole in protease function suggest that this mechanism of Na + activation is present in all Na + -activated trypsin-like proteases.
The molecular mechanism of thrombin activation by Na{sup +} remains elusive. Its kinetic formulation requires extension of the classical Botts-Morales theory for the action of a modifier on an enzyme to correctly account for the contribution of the E*, E, and E:Na{sup +} forms. The extended scheme establishes that analysis of k{sub cat} unequivocally identifies allosteric transduction of Na{sup +} binding into enhanced catalytic activity. The thrombin mutant N143P features no Na{sup +}-dependent enhancement of k{sub cat} yet binds Na{sup +} with an affinity comparable to that of wild type. Crystal structures of the mutant in the presence and absence of Na{sup +} confirm that Pro{sup 143} abrogates the important H-bond between the backbone N atom of residue 143 and the carbonyl O atom of Glu{sup 192}, which in turn controls the orientation of the Glu{sup 192}-Gly{sup 193} peptide bond and the correct architecture of the oxyanion hole. We conclude that Na{sup +} activates thrombin by securing the correct orientation of the Glu{sup 192}-Gly{sup 193} peptide bond, which is likely flipped in the absence of cation. Absolute conservation of the 143-192 H-bond in trypsin-like proteases and the importance of the oxyanion hole in protease function suggest that this mechanism of Na{sup +} activation is present in all Na{sup +}-activated trypsin-like proteases.
The molecular mechanism of thrombin activation by Na⁺ remains elusive. Its kinetic formulation requires extension of the classical Botts-Morales theory for the action of a modifier on an enzyme to correctly account for the contribution of the E*, E, and E:Na⁺ forms. The extended scheme establishes that analysis of kcat unequivocally identifies allosteric transduction of Na⁺ binding into enhanced catalytic activity. The thrombin mutant N143P features no Na⁺-dependent enhancement of kcat yet binds Na⁺ with an affinity comparable to that of wild type. Crystal structures of the mutant in the presence and absence of Na⁺ confirm that Pro¹⁴³ abrogates the important H-bond between the backbone N atom of residue 143 and the carbonyl O atom of Glu¹⁹², which in turn controls the orientation of the Glu¹⁹²-Gly¹⁹³ peptide bond and the correct architecture of the oxyanion hole. We conclude that Na⁺ activates thrombin by securing the correct orientation of the Glu¹⁹²-Gly¹⁹³ peptide bond, which is likely flipped in the absence of cation. Absolute conservation of the 143-192 H-bond in trypsin-like proteases and the importance of the oxyanion hole in protease function suggest that this mechanism of Na⁺ activation is present in all Na⁺-activated trypsin-like proteases.
The molecular mechanism of thrombin activation by Na(+) remains elusive. Its kinetic formulation requires extension of the classical Botts-Morales theory for the action of a modifier on an enzyme to correctly account for the contribution of the E*, E, and E:Na(+) forms. The extended scheme establishes that analysis of k(cat) unequivocally identifies allosteric transduction of Na(+) binding into enhanced catalytic activity. The thrombin mutant N143P features no Na(+)-dependent enhancement of k(cat) yet binds Na(+) with an affinity comparable to that of wild type. Crystal structures of the mutant in the presence and absence of Na(+) confirm that Pro(143) abrogates the important H-bond between the backbone N atom of residue 143 and the carbonyl O atom of Glu(192), which in turn controls the orientation of the Glu(192)-Gly(193) peptide bond and the correct architecture of the oxyanion hole. We conclude that Na(+) activates thrombin by securing the correct orientation of the Glu(192)-Gly(193) peptide bond, which is likely flipped in the absence of cation. Absolute conservation of the 143-192 H-bond in trypsin-like proteases and the importance of the oxyanion hole in protease function suggest that this mechanism of Na(+) activation is present in all Na(+)-activated trypsin-like proteases.
The molecular mechanism of thrombin activation by Na+ remains elusive. Its kinetic formulation requires extension of the classical Botts-Morales theory for the action of a modifier on an enzyme to correctly account for the contribution of the E*, E, and E:Na+ forms. The extended scheme establishes that analysis of kcat unequivocally identifies allosteric transduction of Na+ binding into enhanced catalytic activity. The thrombin mutant N143P features no Na+-dependent enhancement of kcat yet binds Na+ with an affinity comparable to that of wild type. Crystal structures of the mutant in the presence and absence of Na+ confirm that Pro143 abrogates the important H-bond between the backbone N atom of residue 143 and the carbonyl O atom of Glu192, which in turn controls the orientation of the Glu192-Gly193 peptide bond and the correct architecture of the oxyanion hole. We conclude that Na+ activates thrombin by securing the correct orientation of the Glu192-Gly193 peptide bond, which is likely flipped in the absence of cation. Absolute conservation of the 143–192 H-bond in trypsin-like proteases and the importance of the oxyanion hole in protease function suggest that this mechanism of Na+ activation is present in all Na+-activated trypsin-like proteases.
Author Chen, Zhiwei
Gandhi, Prafull S.
Niu, Weiling
Bah, Alaji
Di Cera, Enrico
Bush-Pelc, Leslie A.
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  surname: Niu
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  givenname: Leslie A.
  surname: Bush-Pelc
  fullname: Bush-Pelc, Leslie A.
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  surname: Di Cera
  fullname: Di Cera, Enrico
  email: enrico@wustl.edu
BackLink https://www.ncbi.nlm.nih.gov/pubmed/19846563$$D View this record in MEDLINE/PubMed
https://www.osti.gov/biblio/1006016$$D View this record in Osti.gov
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SSID ssj0000491
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Snippet The molecular mechanism of thrombin activation by Na+ remains elusive. Its kinetic formulation requires extension of the classical Botts-Morales theory for the...
The molecular mechanism of thrombin activation by Na⁺ remains elusive. Its kinetic formulation requires extension of the classical Botts-Morales theory for the...
The molecular mechanism of thrombin activation by Na + remains elusive. Its kinetic formulation requires extension of the classical Botts-Morales theory for...
The molecular mechanism of thrombin activation by Na(+) remains elusive. Its kinetic formulation requires extension of the classical Botts-Morales theory for...
The molecular mechanism of thrombin activation by Na{sup +} remains elusive. Its kinetic formulation requires extension of the classical Botts-Morales theory...
The molecular mechanism of thrombin activation by Na + remains elusive. Its kinetic formulation requires extension of the classical Botts-Morales theory for...
SourceID pubmedcentral
osti
crossref
pubmed
highwire
fao
elsevier
SourceType Open Access Repository
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Publisher
StartPage 36175
SubjectTerms AFFINITY
Allosteric Regulation - genetics
Amino Acid Substitution
ARCHITECTURE
ATOMS
CARBONYLS
CRYSTAL STRUCTURE
Crystallography, X-Ray
Enzyme Activation - genetics
Enzyme Catalysis and Regulation
ENZYMES
Humans
Hydrogen Bonding
KINETICS
MATERIALS SCIENCE
MUTANTS
Mutation, Missense
ORIENTATION
PEPTIDES
Protein Binding - genetics
Protein Structure, Tertiary - physiology
RESIDUES
Sodium - chemistry
Sodium - metabolism
Structure-Activity Relationship
THROMBIN
Thrombin - chemistry
Thrombin - genetics
Thrombin - metabolism
Title Mutant N143P Reveals How Na+ Activates Thrombin
URI https://dx.doi.org/10.1074/jbc.M109.069500
http://www.jbc.org/content/284/52/36175.abstract
https://www.ncbi.nlm.nih.gov/pubmed/19846563
https://www.osti.gov/biblio/1006016
https://pubmed.ncbi.nlm.nih.gov/PMC2794733
Volume 284
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