Subunit structure of dipeptidyl transferase

Metrione, Robert M.; Okuda, Yoshihiro; Fairclough, Gordon F.

doi:10.1021/bi00814a006

Cited by 24 publications

(13 citation statements)

References 23 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…This is further supported by the finding that monomeric procathepsin C (55 kDa) is only slightly larger than the monomeric form of the mature enzyme (Fig. 1A) or of the intermediate of 53 kDa (14), which presumably corresponded to the monomeric form. Although this finding is unusual for lysosomal cysteine proteinases, where only cathepsin H is a slight exception (41,42), it is well known that large parts of proregions can remain bound to the active form of an enzyme.…”

Section: Fig 4 Substrate Inhibition Of Human Cathepsin C Modelled Bysupporting

confidence: 67%

“…When dissociation of bovine cathepsin C was studied in the presence of guanidinium chloride and urea (14), an intermediate with a molecular mass of 53 kDa was observed, which could be further dissociated into smaller subunits with molecular mass of 24.5 kDa, suggesting that cathepsin C consists of eight subunits. Furthermore, two different NH 2 -terminal amino acids were found, suggesting that two different types of subunits are present in the enzyme.…”

Section: Discussionmentioning

confidence: 99%

“…Cathepsin C is also inhibited by rat stefin A and chicken cystatin, two protein inhibitors of cysteine peptidases from the cystatin superfamily (2,19). There are differing reports concerning the molecular mass and subunit composition of cathepsin C. Thus bovine cathepsin C was found to be an oligomeric enzyme of about 200 kDa, composed of eight subunits in the form of two tetramers with two different types of subunits (14). The rat liver enzyme was also estimated to have a molecular mass of 200 kDa (12), but more recently 160 kDa, consisting of two different subunits (2).…”

mentioning

confidence: 99%

See 2 more Smart Citations

Oligomeric Structure and Substrate Induced Inhibition of Human Cathepsin C

Dolenc

Turk

Pungerčič

et al. 1995

Journal of Biological Chemistry

118

View full text Add to dashboard Cite

Cathepsin C has been purified from human kidney by a modified procedure. Human cathepsin C was isolated as pure protein with a pI close to 6.0. The enzyme was shown to have a molecular mass of 200 kDa and to consist of four identical subunits, each composed of three different polypeptide chains, two of them disulfidebound. Their NH 2 -terminal amino acid sequences were determined. Two chains showed pronounced similarity with the heavy and light chains of other papain-like cysteine proteinases, whereas the third one corresponded to the prosequence of the enzyme, thus showing that a substantial part of the proregion remains bound in the mature enzyme. The kinetics of substrate hydrolysis deviated substantially from standard Michaelis-Menten kinetics, demonstrating substrate inhibition at higher substrate concentrations. These data are explained by a sequential cooperative interaction model, where an enzyme molecule can bind up to four substrate molecules but where only the binary enzymesubstrate complex is catalytically active. Substrate inhibition was observed over the whole range of pH activity. From the pH activity profile it can be concluded that at least three ionizable groups with pK a values 4.2, 6.8, and 7.7 are involved in substrate hydrolysis. Human cathepsin C thus appears to differ qualitatively from other cysteine proteinases of different origin.

show abstract

Section: Fig 4 Substrate Inhibition Of Human Cathepsin C Modelled Bysupporting

confidence: 67%

Section: Discussionmentioning

confidence: 99%

mentioning

confidence: 99%

See 1 more Smart Citation

Oligomeric Structure and Substrate Induced Inhibition of Human Cathepsin C

Dolenc

Turk

Pungerčič

et al. 1995

Journal of Biological Chemistry

118

View full text Add to dashboard Cite

show abstract

“…The purified enzyme showed a monomer, such character that corresponds with cathepsin S purified from different species and tissues and also with papain 2,22 . This physical property makes cathepsin S distinct from other lysosomal cysteine proteases such as cathepsins B, L, and H which are two chain forms, 7,23 together with cathepsin C which has more than two subunits 24 …”

Section: Discussionmentioning

confidence: 88%

Purification and characterization of cathepsin S from hepatopancreas of carp Cyprinus carpio

et al. 2000

View full text Add to dashboard Cite

SUMMARY: Cathepsin S was purified from carp hepatopancreas to homogeneity up to 300‐fold. The amino acid sequence of its NH2‐terminus was determined to be V‐P‐D‐A‐M‐D‐W‐Y‐N‐K‐G‐Y‐V‐T‐D‐V‐K‐N‐Q. On the contrary, that of purified cathepsin L from carp hepatopancreas was to be V‐P‐N‐S‐L‐D‐W‐R‐E‐K‐G. Purified cathepsin S consisted of a single chain with 37 kDa estimated by sodium dodecylsulfate–polyacrylamide gel electrophoresis. The enzyme had strong hydrolytic activity toward Z‐Phe‐Arg‐MCA with the pH optimum of 7.0, but this lacked the ability to hydrolyze most of the other MCA substrates. The optimum pH of cathepsin S for protein substrate (carp myosin heavy chain) was also to be pH 7.0. These properties of purified cathepsin S obviously differ from cathepsins B and L. The enzyme activity was totally inhibited by E‐64, leupeptin, 5–5′‐dithiobis (2‐nitro‐benzoic acid) and p‐tosyl‐lys chloromethylketone as well.

show abstract

“…DPPI is capable of sequentially removing dipeptides from the amino termini of various peptides and protein substrates (3)(4)(5)(6)(7) and, along with other cysteine proteases, is thought to play an important role in intracellular protein degradation and turnover (4,8,9). This enzyme has other postulated functions, including involvement in cell growth (10), neuraminidase activation (11), and platelet factor XIII activation (12).…”

mentioning

confidence: 99%

Molecular Cloning, Chromosomal Localization, and Expression of Murine Dipeptidyl Peptidase I

Pham

Armstrong

Zimonjic

et al. 1997

Journal of Biological Chemistry

View full text Add to dashboard Cite

Dipeptidyl peptidase I (DPPI) is a lysosomal cysteine protease that catalyzes the sequential removal of dipeptides from the amino termini of various protein substrates. We have isolated a cDNA coding for murine DPPI from mouse thymus and spleen cDNA libraries. The deduced amino acid sequence codes for a protein of 462 amino acid residues; comparison of this deduced sequence with that of rat and human DPPI revealed 90.1% and 77.8% identity, respectively. Using DPPI cDNA, we obtained two BAC (Bacterial Artificial Chromosome) clones that contained the murine DPPI locus. The DPPI gene consists of seven exons and 6 introns, and spans approximately 20 kilobases. Using fluorescence in situ chromosome hybridization, we localized murine DPPI to chromosome 7D3-E1.1. We determined that DPPI protein is widely distributed in mouse tissues, although its relative abundance varies from tissue to tissue. In contrast to previous reports, we show here that DPPI mRNA and protein levels and enzymatic activity are unchanged during in vitro T cell activation, implying that this enzyme is not rate-limiting for granzyme processing.

show abstract

Subunit structure of dipeptidyl transferase

Cited by 24 publications

References 23 publications

Oligomeric Structure and Substrate Induced Inhibition of Human Cathepsin C

Oligomeric Structure and Substrate Induced Inhibition of Human Cathepsin C

Purification and characterization of cathepsin S from hepatopancreas of carp Cyprinus carpio

Molecular Cloning, Chromosomal Localization, and Expression of Murine Dipeptidyl Peptidase I

Contact Info

Product

Resources

About