Modification of the catalytic subunit of bovine heart cAMP-dependent protein kinase with affinity labels related to peptide substrates.

Bramson, H. Neal; Thomas, Nancy E.; Matsueda, Rei; Nelson, Nicole; Taylor, Susan S.; Kaiser, E. T.

doi:10.1016/s0021-9258(18)33860-2

Cited by 90 publications

(21 citation statements)

References 30 publications

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“…Earlier work with affinity peptide 6, which undergoes disulfide interchange with the sulfhydryl groups in the catalytic subunit, identified Cys-199 as the site of labeling (Bramson et al, 1982). Furthermore, attachment of one peptide residue H ?…”

Section: Discussionmentioning

confidence: 99%

“…The catalytic subunit of the cAMP-dependent protein kinase was purified to homogeneity from bovine heart as previously described (Bramson et al, 1982). [ 1 -14C]Bromoacetic acid was purchased from Amersham.…”

Section: Methodsmentioning

confidence: 99%

“…However, only two substrate-based affinity inactivators, one an ATP analogue and the other a peptide 1 analogue, have been studied thoroughly with this enzyme. By this approach lysine-72 (Zoller et al, 1981) and cysteine-199 (Bramson et al, 1982) have been shown to be at or near the active site. To probe further the nature of other active-site amino acid residues, we have substituted systematically amino acid residues in the primary sequence of peptide 1 by amino acid analogues that can act as electrophiles.…”

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confidence: 99%

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Identification of amino acid residues involved in substrate recognition by the catalytic subunit of bovine cyclic AMP dependent protein kinase: peptide-based affinity labels

Mobashery¹,

Kaiser²

1988

Biochemistry

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Two peptide-based affinity inactivators Ac-Leu-(BrAc)Orn-Arg-Ala-Ser-Leu-Gly (4) and Ac-Leu-Arg-(BrAc)Orn-Ala-Ser-Leu-Gly (5) were prepared as probes for the study of the nature of the active-site residues in the catalytic subunit of cyclic AMP dependent protein kinase. Under conditions of inhibitor in excess, both peptides inactivated the catalytic subunit by an apparent biphasic process. A fast phase, which inactivated the protein by approximately 40%, was followed by a slow phase that accounted for the loss of the remaining enzyme activity. Protection experiments with the kinase substrates showed that the slow phase of inactivation was active site directed, while the fast phase was not. Studies with radioactively labeled peptides 4 and 5 indicated incorporation of two peptide residues per molecule of the catalytic subunit upon complete inactivation. This observation is consistent with the occurrence of one alkylation event in each phase of the inactivation. The protein was proteolyzed subsequent to its modification with radioactive peptides. High-performance liquid chromatography afforded two radioactive peptide fragments in each case, which were sequenced by Edman degradation. Peptide 4 alkylated Thr-197 and Glu-346, while peptide 5 modified Cys-199 and also Glu-346. Data are presented to support the conclusion that Thr-197 and Cys-199 are located at or near the active site.

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Section: Discussionmentioning

confidence: 99%

Section: Methodsmentioning

confidence: 99%

mentioning

confidence: 99%

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Identification of amino acid residues involved in substrate recognition by the catalytic subunit of bovine cyclic AMP dependent protein kinase: peptide-based affinity labels

Mobashery¹,

Kaiser²

1988

Biochemistry

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“…In particular, a stretch of very high (75%) homology to the insulin receptor exists between positions 245 and 288 in rosi, which can be aligned with positions 178 to 215 in the cyclic AMP-dependent protein kinase. Since Cys-198 of the cyclic AMP-dependent protein kinase is protected from chemical modification by peptide substrates, this region has been implicated in substrate binding (5). The high degree of homology between the amino acid sequences of rosl and the insulin receptor in this putative substrate-binding domain might indicate a similar substrate specificity for the tyrosine kinase activities of these two proteins.…”

Section: Discussionmentioning

confidence: 99%

Characterization of an Activated Human ros Gene

Birchmeier¹,

Birnbaum

Waitches

et al. 1986

Molecular and Cellular Biology

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A human oncogene, mcf3, previously detected by a combination of DNA-mediated gene transfer and a tumorigenicity assay, derives from a human homology of the avian v-ros oncogene. Both v-ros and mcf3 can encode a protein with homology to tyrosine-specific protein kinases, and both mcf3 and v-ros encode a potential transmembrane domain N terminal to the kinase domain. mcf3 probably arose during gene transfer from a normal human ros gene by the loss of a putative extracellular domain. There do not appear to be any other gross rearrangements in the structure of mcf3.

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“…serves as catalytically active reference kinases, since crystal structure of its kinase domain is well characterised (Bramson et al, 1982;Engh et al, 1996;Prade et al, 1997;Davies et al, 2007). EFR and CERK1 represent typical immune related A. thaliana receptor-like kinases with experimentally proven phosphorylation activity (Schwessinger et al, 2011;Suzuki et al, 2016).…”

Section: In Silico Analyses Suggest That At5g24080 Is An Active G-typ...mentioning

confidence: 99%

Identification of Arabidopsis genes involved in differential interaction phenotype establishment by distinct Verticillium spp. and isolates

Stepanets¹

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Modification of the catalytic subunit of bovine heart cAMP-dependent protein kinase with affinity labels related to peptide substrates.

Cited by 90 publications

References 30 publications

Identification of amino acid residues involved in substrate recognition by the catalytic subunit of bovine cyclic AMP dependent protein kinase: peptide-based affinity labels

Identification of amino acid residues involved in substrate recognition by the catalytic subunit of bovine cyclic AMP dependent protein kinase: peptide-based affinity labels

Characterization of an Activated Human ros Gene

Identification of Arabidopsis genes involved in differential interaction phenotype establishment by distinct Verticillium spp. and isolates

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