Easily polarizable proton transfer hydrogen bonds between the side chains of histidine and the carboxylic acid groups of glutamic and aspartic acid residues in proteins

Rastogi, Pushti Prakash; Kristof, Wolfgang; Zuńdel, Georg

doi:10.1016/0141-8130(81)90056-8

Cited by 18 publications

(1 citation statement)

References 17 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Since an X-ray structure of DP IV could not be obtained up till now we proceed this way to get some structure information. With some exceptions, most previous models of substrate hydrolysis by serine proteases have tended to describe the amide cleaving mechanism without regard for a possible interaction between the catalytic action and the specificity for substrates [12][13][14][15][16][17][18][19][20][21][22][23][24]. In view of the high substrate specificity of DP IV, we decided to study the conformations of several substrates and 'nonsubstrates', hoping to find one structure which could explain, on the one hand, the substrate specificity of DP IV and, on the other hand, the first important step of the hydrolysis mechanism of DP IV.…”

Section: Introductionmentioning

confidence: 99%

The probable conformation of substrates recognized by dipeptidyl-peptidase IV and some aspects of the catalytic mechanism derived from theoretical investigations

Brandt

Lehmann

Hofmann

et al. 1992

J Computer-Aided Mol Des

View full text Add to dashboard Cite

By theoretical conformational investigations of substrates and nonsubstrates of the enzyme dipeptidyl-peptidase IV (DP IV) as well as dipeptide-esters using the ECEPP83 method we determined the structure of peptides recognized and cleaved by the enzyme. From a comparison of all possible structures for the substrates with conformations not possible in nonsubstrates we concluded that a single conformation explains substrate specificities of DP IV. This conformation is characterized by the following dihedral angles: psi 1 = 85 degrees, omega 1 = 180 degrees, phi 2 = -75 degrees, psi 2 = 80 degrees, and omega 2 = 180 degrees. The conclusions were supported by comparisons of molecular electrostatic potentials calculated with the molecular graphics program HAMOG.

show abstract

Section: Introductionmentioning

confidence: 99%

The probable conformation of substrates recognized by dipeptidyl-peptidase IV and some aspects of the catalytic mechanism derived from theoretical investigations

Brandt

Lehmann

Hofmann

et al. 1992

J Computer-Aided Mol Des

View full text Add to dashboard Cite

show abstract

Hydrogen Bonds with Large Proton Polarizability and Proton Transfer Processes in Electrochemistry and Biology

Zuńdel¹

1999

Advances in Chemical Physics

196

127

View full text Add to dashboard Cite

Proton transfer and polarizability of hydrogen bonds formed between cysteine and lysine residues

Kristof

Zuńdel

1982

Biopolymers

Self Cite

View full text Add to dashboard Cite

(L‐Cys)n + N‐base systems and (L‐Cys)n + (L‐Lys)n systems were studied by ir spectroscopy. It is shown that in the water‐free systems, SH ⃛N ⇌ S− ⃛H+N hydrogen bonds are formed. With the (L‐Cys)n + N‐base systems, both proton‐limiting structures in the SH ⃛N ⇌ S− ⃛H+N bonds have equal weight when the pKa of the protonated N‐base is 2 pKa units larger than that of (L‐Cys)n. The same is true with the water‐free (L‐Cys)n + (L‐Lys)n system. Thus, with regard to the type of proton potentials present, these hydrogen bonds are proton‐transfer hydrogen bonds showing very large proton polarizabilities. This is confirmed by the occurrence of continua in the ir spectra. Small amounts of water open these hydrogen bonds and increase the transfer of the proton to (L‐Lys)n. In the (L‐Lys)n + N‐base systems, with increasing proton transfer the backbone of (L‐Cys)n changes from antiparallel β‐structure to coil. In (L‐Cys)n + (L‐Lys)n, the conformation is determined by the (L‐Lys)n conformation and changes depending on the chain length of (L‐Lys)n. Finally, the reactivity increase in the active center of fatty acid synthetase, which should be caused by the shift of a proton, is discussed on the basis of the great proton polarizability of the cysteine–lysine hydrogen bonds.

show abstract

Easily polarizable proton transfer hydrogen bonds between the side chains of histidine and the carboxylic acid groups of glutamic and aspartic acid residues in proteins

Cited by 18 publications

References 17 publications

The probable conformation of substrates recognized by dipeptidyl-peptidase IV and some aspects of the catalytic mechanism derived from theoretical investigations

The probable conformation of substrates recognized by dipeptidyl-peptidase IV and some aspects of the catalytic mechanism derived from theoretical investigations

Hydrogen Bonds with Large Proton Polarizability and Proton Transfer Processes in Electrochemistry and Biology

Proton transfer and polarizability of hydrogen bonds formed between cysteine and lysine residues

Contact Info

Product

Resources

About