BIOMAT Database Logo BIOMAT Database Logo

Distinct C-terminal sequences of isozymes I and II of the human erythrocyte L-isoaspartyl/D-aspartyl protein methyltransferase. 1991

D Ingrosso, and R M Kagan, and S Clarke
Department of Chemistry and Biochemistry, University of California, Los Angeles 90024-1569.

We have purified the more acidic major isozyme (II) of the human erythrocyte L-isoaspartyl/D-aspartyl methyltransferase and compared its structure to that of the previously sequenced isozyme I. These isozymes are both monomers of 25,000 molecular weight polypeptides and have similar enzymatic properties, but have isoelectric points that differ by one pH unit. Analysis of 16 tryptic peptides of isozyme II accounting for 89% of the sequence of isozyme I revealed no differences between these enzyme forms. However, analysis of a Staphylococcal V8 protease C-terminal fragment revealed that the last two residues of these proteins differed. The Trp-Lys-COOH terminus of isozyme I is replaced by a Asp-Asp-COOH terminus in isozyme II. Southern blot analysis of genomic DNA suggests that the human genome [corrected] may contain only a single gene encoding the enzyme. We propose that the distinct C-termini of isozymes I and II can arise from the generation of multiple mRNA's by alternative splicing.

UI MeSH Term Description Entries
D007527 Isoenzymes Structurally related forms of an enzyme. Each isoenzyme has the same mechanism and classification, but differs in its chemical, physical, or immunological characteristics. Alloenzyme,Allozyme,Isoenzyme,Isozyme,Isozymes,Alloenzymes,Allozymes
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
D010446 Peptide Fragments Partial proteins formed by partial hydrolysis of complete proteins or generated through PROTEIN ENGINEERING techniques. Peptide Fragment,Fragment, Peptide,Fragments, Peptide
D011496 Protein Methyltransferases Enzymes that catalyze the methylation of amino acids after their incorporation into a polypeptide chain. S-Adenosyl-L-methionine acts as the methylating agent. EC 2.1.1. Protein Methylase,Protein Methylases,Protein Methyltransferase,Methylase, Protein,Methylases, Protein,Methyltransferase, Protein,Methyltransferases, Protein
D004912 Erythrocytes Red blood cells. Mature erythrocytes are non-nucleated, biconcave disks containing HEMOGLOBIN whose function is to transport OXYGEN. Blood Cells, Red,Blood Corpuscles, Red,Red Blood Cells,Red Blood Corpuscles,Blood Cell, Red,Blood Corpuscle, Red,Erythrocyte,Red Blood Cell,Red Blood Corpuscle
D006801 Humans Members of the species Homo sapiens. Homo sapiens,Man (Taxonomy),Human,Man, Modern,Modern Man
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
D012689 Sequence Homology, Nucleic Acid The sequential correspondence of nucleotides in one nucleic acid molecule with those of another nucleic acid molecule. Sequence homology is an indication of the genetic relatedness of different organisms and gene function. Base Sequence Homology,Homologous Sequences, Nucleic Acid,Homologs, Nucleic Acid Sequence,Homology, Base Sequence,Homology, Nucleic Acid Sequence,Nucleic Acid Sequence Homologs,Nucleic Acid Sequence Homology,Sequence Homology, Base,Base Sequence Homologies,Homologies, Base Sequence,Sequence Homologies, Base
D014357 Trypsin A serine endopeptidase that is formed from TRYPSINOGEN in the pancreas. It is converted into its active form by ENTEROPEPTIDASE in the small intestine. It catalyzes hydrolysis of the carboxyl group of either arginine or lysine. EC 3.4.21.4. Tripcellim,Trypure,beta-Trypsin,beta Trypsin
D026601 Protein D-Aspartate-L-Isoaspartate Methyltransferase A PROTEIN O-METHYLTRANSFERASE that recognizes and catalyzes the methyl esterification of ISOASPARTIC ACID and D-ASPARTIC ACID residues in peptides and proteins. It initiates the repair of proteins damaged by the spontaneous decomposition of normal L-aspartic acid and L-asparagine residues. Protein-D-Aspartate Methyltransferase,Protein-L-Isoaspartate-D-Aspartate-O-Methyltransferase,D-Aspartyl-L-Isoaspartyl Methyltransferase,Isoaspartyl-Aspartyl Protein Methyltransferase,L-Isoaspartyl Protein Carboxymethyltransferase,Methyltransferase PIMT,PCMT1 Gene Product,Protein L-Isoaspartate O-Methyltransferase,Protein L-Isoaspartyl Methyltransferase,Protein-D-Asp Methyltransferase,Protein-L-Isoaspartate Methyltransferase,Protein-beta-Aspartate Methyltransferase,pcm Gene Product,Carboxymethyltransferase, L-Isoaspartyl Protein,D Aspartyl L Isoaspartyl Methyltransferase,Gene Product, PCMT1,Gene Product, pcm,Isoaspartyl Aspartyl Protein Methyltransferase,L Isoaspartyl Protein Carboxymethyltransferase,L-Isoaspartate O-Methyltransferase, Protein,L-Isoaspartyl Methyltransferase, Protein,Methyltransferase, D-Aspartyl-L-Isoaspartyl,Methyltransferase, Isoaspartyl-Aspartyl Protein,Methyltransferase, Protein D-Aspartate-L-Isoaspartate,Methyltransferase, Protein L-Isoaspartyl,Methyltransferase, Protein-D-Asp,Methyltransferase, Protein-D-Aspartate,Methyltransferase, Protein-L-Isoaspartate,Methyltransferase, Protein-beta-Aspartate,O-Methyltransferase, Protein L-Isoaspartate,PIMT, Methyltransferase,Protein Carboxymethyltransferase, L-Isoaspartyl,Protein D Asp Methyltransferase,Protein D Aspartate L Isoaspartate Methyltransferase,Protein D Aspartate Methyltransferase,Protein L Isoaspartate D Aspartate O Methyltransferase,Protein L Isoaspartate Methyltransferase,Protein L Isoaspartate O Methyltransferase,Protein L Isoaspartyl Methyltransferase,Protein Methyltransferase, Isoaspartyl-Aspartyl,Protein beta Aspartate Methyltransferase

Related Publications

D Ingrosso, and R M Kagan, and S Clarke
Two major isozymes of the protein D-aspartyl/L-isoaspartyl methyltransferase from human erythrocytes.
March 1988, Biochemical and biophysical research communications,
D Ingrosso, and R M Kagan, and S Clarke
Recognition of D-aspartyl residues in polypeptides by the erythrocyte L-isoaspartyl/D-aspartyl protein methyltransferase. Implications for the repair hypothesis.
March 1992, The Journal of biological chemistry,
D Ingrosso, and R M Kagan, and S Clarke
Determination of two sites of automethylation in bovine erythrocyte protein (D-aspartyl/L-isoaspartyl) carboxyl methyltransferase.
January 1996, Journal of protein chemistry,
D Ingrosso, and R M Kagan, and S Clarke
Structure of the human gene encoding the protein repair L-isoaspartyl (D-aspartyl) O-methyltransferase.
November 1996, Archives of biochemistry and biophysics,
D Ingrosso, and R M Kagan, and S Clarke
Chemical conversion of aspartyl peptides to isoaspartyl peptides. A method for generating new methyl-accepting substrates for the erythrocyte D-aspartyl/L-isoaspartyl protein methyltransferase.
September 1986, The Journal of biological chemistry,
D Ingrosso, and R M Kagan, and S Clarke
Amino acid polymorphisms of the human L-isoaspartyl/D-aspartyl methyltransferase involved in protein repair.
August 1994, Biochemical and biophysical research communications,
D Ingrosso, and R M Kagan, and S Clarke
Automethylation of protein (D-aspartyl/L-isoaspartyl) carboxyl methyltransferase, a response to enzyme aging.
January 1994, Journal of protein chemistry,
D Ingrosso, and R M Kagan, and S Clarke
Human erythrocyte D-aspartyl/L-isoaspartyl methyltransferases: enzymes that recognize age-damaged proteins.
January 1991, Advances in experimental medicine and biology,
D Ingrosso, and R M Kagan, and S Clarke
The role of protein L-isoaspartyl/D-aspartyl O-methyltransferase (PIMT) in intracellular signal transduction.
June 2010, Chemistry & biodiversity,
D Ingrosso, and R M Kagan, and S Clarke
Structural elements affecting the recognition of L-isoaspartyl residues by the L-isoaspartyl/D-aspartyl protein methyltransferase. Implications for the repair hypothesis.
October 1991, The Journal of biological chemistry,
Copied contents to your clipboard!