BIOMAT Database Logo BIOMAT Database Logo

The amine-donor substrate specificity of tissue-type transglutaminase. Influence of amino acid residues flanking the amine-donor lysine residue. 1994

P J Groenen, and R H Smulders, and R F Peters, and J J Grootjans, and P R van den Ijssel, and H Bloemendal, and W W de Jong
Department of Biochemistry, University of Nijmegen, The Netherlands.

The amine-donor substrate specificity of tissue-type transglutaminase has been studied in a series of recombinant alpha A-crystallin mutants. These mutant proteins have been provided with a potential substrate lysine residue, flanked by different amino acid residues, in the C-terminal extended arm of alpha A-crystallin. A biotinylated amine-acceptor hexapeptide was used as a probe for labelling the amine-donor sites. Wild-type bovine alpha A-crystallin does not function as an amine-donor substrate for tissue-type transglutaminase. Yet, upon introduction of a lysine residue at the C-terminal or penultimate position, all mutant alpha A-crystallins act as amine-donor substrates, although to different extents. This shows that accessibility is the primary requirement for a lysine residue to function as an amine-donor substrate for transglutaminase and that the enzyme has a broad tolerance towards the neighbouring residues. However, the nature of the flanking amino acid residues does clearly affect the reactivity of the substrate lysine residue. Notably, we found that a proline or glycine residue in front of the substrate lysine has a strong adverse effect on the substrate reactivity as compared to a preceding leucine, serine, alanine or arginine residue.

UI MeSH Term Description Entries
D008239 Lysine An essential amino acid. It is often added to animal feed. Enisyl,L-Lysine,Lysine Acetate,Lysine Hydrochloride,Acetate, Lysine,L Lysine
D008969 Molecular Sequence Data Descriptions of specific amino acid, carbohydrate, or nucleotide sequences which have appeared in the published literature and/or are deposited in and maintained by databanks such as GENBANK, European Molecular Biology Laboratory (EMBL), National Biomedical Research Foundation (NBRF), or other sequence repositories. Sequence Data, Molecular,Molecular Sequencing Data,Data, Molecular Sequence,Data, Molecular Sequencing,Sequencing Data, Molecular
D011503 Transglutaminases Transglutaminases catalyze cross-linking of proteins at a GLUTAMINE in one chain with LYSINE in another chain. They include keratinocyte transglutaminase (TGM1 or TGK), tissue transglutaminase (TGM2 or TGC), plasma transglutaminase involved with coagulation (FACTOR XIII and FACTOR XIIIa), hair follicle transglutaminase, and prostate transglutaminase. Although structures differ, they share an active site (YGQCW) and strict CALCIUM dependence. Glutaminyl-Peptide Gamma-Glutamyltransferases,Protein-Glutamine gamma-Glutamyltransferases,Transglutaminase,Gamma-Glutamyltransferases, Glutaminyl-Peptide,Glutaminyl Peptide Gamma Glutamyltransferases,Protein Glutamine gamma Glutamyltransferases,gamma-Glutamyltransferases, Protein-Glutamine
D002417 Cattle Domesticated bovine animals of the genus Bos, usually kept on a farm or ranch and used for the production of meat or dairy products or for heavy labor. Beef Cow,Bos grunniens,Bos indicus,Bos indicus Cattle,Bos taurus,Cow,Cow, Domestic,Dairy Cow,Holstein Cow,Indicine Cattle,Taurine Cattle,Taurus Cattle,Yak,Zebu,Beef Cows,Bos indicus Cattles,Cattle, Bos indicus,Cattle, Indicine,Cattle, Taurine,Cattle, Taurus,Cattles, Bos indicus,Cattles, Indicine,Cattles, Taurine,Cattles, Taurus,Cow, Beef,Cow, Dairy,Cow, Holstein,Cows,Dairy Cows,Domestic Cow,Domestic Cows,Indicine Cattles,Taurine Cattles,Taurus Cattles,Yaks,Zebus
D003459 Crystallins A heterogeneous family of water-soluble structural proteins found in cells of the vertebrate lens. The presence of these proteins accounts for the transparency of the lens. The family is composed of four major groups, alpha, beta, gamma, and delta, and several minor groups, which are classed on the basis of size, charge, immunological properties, and vertebrate source. Alpha, beta, and delta crystallins occur in avian and reptilian lenses, while alpha, beta, and gamma crystallins occur in all other lenses. Lens Proteins,Crystallin,Eye Lens Protein,Lens Protein, Eye,Protein, Eye Lens,Proteins, Lens
D000595 Amino Acid Sequence The order of amino acids as they occur in a polypeptide chain. This is referred to as the primary structure of proteins. It is of fundamental importance in determining PROTEIN CONFORMATION. Protein Structure, Primary,Amino Acid Sequences,Sequence, Amino Acid,Sequences, Amino Acid,Primary Protein Structure,Primary Protein Structures,Protein Structures, Primary,Structure, Primary Protein,Structures, Primary Protein
D000818 Animals Unicellular or multicellular, heterotrophic organisms, that have sensation and the power of voluntary movement. Under the older five kingdom paradigm, Animalia was one of the kingdoms. Under the modern three domain model, Animalia represents one of the many groups in the domain EUKARYOTA. Animal,Metazoa,Animalia
D001483 Base Sequence The sequence of PURINES and PYRIMIDINES in nucleic acids and polynucleotides. It is also called nucleotide sequence. DNA Sequence,Nucleotide Sequence,RNA Sequence,DNA Sequences,Base Sequences,Nucleotide Sequences,RNA Sequences,Sequence, Base,Sequence, DNA,Sequence, Nucleotide,Sequence, RNA,Sequences, Base,Sequences, DNA,Sequences, Nucleotide,Sequences, RNA
D013329 Structure-Activity Relationship The relationship between the chemical structure of a compound and its biological or pharmacological activity. Compounds are often classed together because they have structural characteristics in common including shape, size, stereochemical arrangement, and distribution of functional groups. Relationship, Structure-Activity,Relationships, Structure-Activity,Structure Activity Relationship,Structure-Activity Relationships
D013379 Substrate Specificity A characteristic feature of enzyme activity in relation to the kind of substrate on which the enzyme or catalytic molecule reacts. Specificities, Substrate,Specificity, Substrate,Substrate Specificities

Related Publications

P J Groenen, and R H Smulders, and R F Peters, and J J Grootjans, and P R van den Ijssel, and H Bloemendal, and W W de Jong
Substrate requirements for transglutaminases. Influence of the amino acid residue preceding the amine donor lysine in a native protein.
September 1995, The Journal of biological chemistry,
P J Groenen, and R H Smulders, and R F Peters, and J J Grootjans, and P R van den Ijssel, and H Bloemendal, and W W de Jong
The carboxy-terminal lysine of alpha B-crystallin is an amine-donor substrate for tissue transglutaminase.
April 1992, European journal of biochemistry,
P J Groenen, and R H Smulders, and R F Peters, and J J Grootjans, and P R van den Ijssel, and H Bloemendal, and W W de Jong
Identification of the amino acid residues conferring substrate specificity upon Selenomonas ruminantium lysine decarboxylase.
October 1999, Bioscience, biotechnology, and biochemistry,
P J Groenen, and R H Smulders, and R F Peters, and J J Grootjans, and P R van den Ijssel, and H Bloemendal, and W W de Jong
Beta B1 crystallin is an amine-donor substrate for tissue transglutaminase.
August 1987, Experimental cell research,
P J Groenen, and R H Smulders, and R F Peters, and J J Grootjans, and P R van den Ijssel, and H Bloemendal, and W W de Jong
The specificity of transglutaminase. II. Structural requirements of the amine substrate.
July 1968, Archives of biochemistry and biophysics,
P J Groenen, and R H Smulders, and R F Peters, and J J Grootjans, and P R van den Ijssel, and H Bloemendal, and W W de Jong
Role of amino-acid residue 95 in substrate specificity of phosphagen kinases.
August 2004, FEBS letters,
P J Groenen, and R H Smulders, and R F Peters, and J J Grootjans, and P R van den Ijssel, and H Bloemendal, and W W de Jong
Alteration of the amino acid substrate specificity of clostridial glutamate dehydrogenase by site-directed mutagenesis of an active-site lysine residue.
February 1995, Protein engineering,
P J Groenen, and R H Smulders, and R F Peters, and J J Grootjans, and P R van den Ijssel, and H Bloemendal, and W W de Jong
Kinetic characterization of yeast alcohol dehydrogenases. Amino acid residue 294 and substrate specificity.
March 1987, The Journal of biological chemistry,
P J Groenen, and R H Smulders, and R F Peters, and J J Grootjans, and P R van den Ijssel, and H Bloemendal, and W W de Jong
Amino acid residues important for substrate specificity of the amino acid permeases Can1p and Gnp1p in Saccharomyces cerevisiae.
November 2001, Yeast (Chichester, England),
P J Groenen, and R H Smulders, and R F Peters, and J J Grootjans, and P R van den Ijssel, and H Bloemendal, and W W de Jong
Amino acid residues contributing to the substrate specificity of the influenza A virus neuraminidase.
August 1999, Journal of virology,
Copied contents to your clipboard!