Amino-Acid Sequence of Bovine Chymotrypsinogen-A

Hartley, B. S.

doi:10.1038/2011284a0

Cited by 373 publications

(124 citation statements)

References 6 publications

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“…Amino acid sequence analysis for MyxSP-1 showed 3 catalytic sequences (His-54, Asp-248, Ser-310) that are characteristic for serine proteases (Hartley 1964). Additional sequence data obtained by 5' and 3' RACE amplification allowed a prediction of the open reading frame for MyxSP-1.…”

Section: Myxsp-1 Sequence Analysismentioning

confidence: 95%

Identification of a serine protease gene expressed by Myxobolus cerebralis during development in rainbow trout Oncorhynchus mykiss

et al. 2004

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Serine proteases have been recognized as key factors in parasite physiology and disease development. We have identified a serine protease gene from Myxobolus cerebralis, MyxSP-1, the myxozoan parasite causing whirling disease in salmonid fishes. The amino acid sequence, as deduced from the cDNA sequence, included a catalytic residue arrangement similar to that of the chymotrypsin family of serine proteases. A real-time TaqMan polymerase chain reaction (PCR) analysis revealed differences in the transcription levels for the chymotrypsin-like protease as found in early, intermediate, and late developmental stages of the parasite in experimentally-infected rainbow trout Oncorhynchus mykiss. MyxSP-1 transcription differed between individual tissues at each sampling point and in the same tissues over time (p < 0.0001). A nonradioactive mRNA in situ hybridization (ISH) protocol was developed to detect MyxSP-1 transcripts. Using a mixture of 3 digoxigenin-labeled antisense mRNA probes, MyxSP-1 transcription was observed in developmental stages of the parasite during the acute and chronic phases of the disease over a 240 d time period in infected rainbow trout tissues. MyxSP-1 transcription observed by ISH in cartilage and as associated with cartilage destruction was consistent with our real-time TaqMan PCR findings that demonstrated high levels of MyxSP-1 transcription during lesion development. Identifying genes encoding these enzymes and characterization of their functions can lead to the development of new chemotherapeutic protocols and vaccine approaches to control parasitic diseases.

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Section: Myxsp-1 Sequence Analysismentioning

confidence: 95%

Identification of a serine protease gene expressed by Myxobolus cerebralis during development in rainbow trout Oncorhynchus mykiss

et al. 2004

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“…Protein Preparation-Initial trials to produce homogenous protein including the residues of the chemical sequence of the hK6 precursor Ala 10 -Lys 245 (chymotrypsin numbering (18); corresponds to Ala 16 -Lys 244 of the sequential protein numbering (see Fig. 1)) failed due to autolysis after Arg 76 .…”

Section: Methodsmentioning

confidence: 99%

The Structure of Human Prokallikrein 6 Reveals a Novel Activation Mechanism for the Kallikrein Family

Gomis‐Rüth¹,

Bayés²,

Sotiropoulou³

et al. 2002

Journal of Biological Chemistry

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Zyme/protease M/neurosin/human kallikrein 6 (hK6) is a member of the human kallikrein family of trypsinlike serine proteinases and was originally identified as being down-regulated in metastatic breast and ovarian tumors when compared with corresponding primary tumors. Recent evidence suggests that hK6 may serve as a circulating tumor marker in ovarian cancers. In addition, it was described in the brain of Parkinson's disease and Alzheimer's disease patients, where it is implicated in amyloid precursor protein processing. It is thus a biomarker for these diseases. To examine the mechanism of activation of hK6, we have solved the structure of its proform, the first of a human kallikrein family member. The proenzyme displays a fold that exhibits chimeric features between those of trypsinogen and other family members. It lacks the characteristic "kallikrein loop" and forms the six disulfide bridges of trypsin. Pro-hK6 displays a completely closed specificity pocket and a unique conformation of the regions involved in structural rearrangements upon proteolytic cleavage activation. This points to a novel activation mechanism, which could be extrapolated to other human kallikreins.

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“…Trypsin, Cat-H and PV 3Cpro belong to 3 distinct families of proteases; upon comparing the sequences of other members of these families, we did not find the same principal catalytic residues (Ser or Cys), a reasonable similarity was observed ( fig.3) ; unpublished), the aligned segments represent the most highly conserved region of the molecules. In cellular serine and cysteine proteinases, these segments form topologically distinct loops [43,44]. The tertiary structure of the viral proteinases discussed here is unknown, but theoretical predictions of their secondary structure suggest that the region in question forms a &fold similar to the serine loop of chymotrypsin-like proteinases.…”

Section: Resultsmentioning

confidence: 99%

Poliovirus‐encoded proteinase 3C: a possible evolutionary link between cellular serine and cysteine proteinase families

1986

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Here we demonstrate significant similarities between the amino acid sequences of trypsin (a serine protease) and the N-terminal piece of a specific fragment of the poliovirus polyprotein encompassing the sequence of the viral proteinase 3C, and also between cathepsin H (a cysteine protease) and the C-terminal piece of the same fragment. A coherent alignment of the sequences of the 3 proteases was obtained, in which the principal catalytically active residues occupy identical positions. A hypothesis is proposed that the viral enzyme may provide an evolutionary link between serine and cysteine protease families.

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Amino-Acid Sequence of Bovine Chymotrypsinogen-A

Cited by 373 publications

References 6 publications

Identification of a serine protease gene expressed by Myxobolus cerebralis during development in rainbow trout Oncorhynchus mykiss

Identification of a serine protease gene expressed by Myxobolus cerebralis during development in rainbow trout Oncorhynchus mykiss

The Structure of Human Prokallikrein 6 Reveals a Novel Activation Mechanism for the Kallikrein Family

Poliovirus‐encoded proteinase 3C: a possible evolutionary link between cellular serine and cysteine proteinase families

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