98 related articles for article (PubMed ID: 17511606)
1. Structural principles of the wide substrate specificity of Thermoactinomyces vulgaris carboxypeptidase T. Reconstruction of the carboxypeptidase B primary specificity pocket.
Akparov VKh; Grishin AM; Yusupova MP; Ivanova NM; Chestukhina GG
Biochemistry (Mosc); 2007 Apr; 72(4):416-23. PubMed ID: 17511606
[TBL] [Abstract][Full Text] [Related]
2. Crystal structure of mutant carboxypeptidase T from Thermoactinomyces vulgaris with an implanted S1' subsite from pancreatic carboxypeptidase B.
Akparov VK; Timofeev VI; Kuranova IP; Rakitina TV
Acta Crystallogr F Struct Biol Commun; 2018 Oct; 74(Pt 10):638-643. PubMed ID: 30279315
[TBL] [Abstract][Full Text] [Related]
3. Structural principles of the broad substrate specificity of Thermoactinomyces vulgaris carboxypeptidase T--role of amino acid residues at positions 260 and 262.
Grishin AM; Akparov VKh; Chestukhina GG
Protein Eng Des Sel; 2008 Sep; 21(9):545-51. PubMed ID: 18515300
[TBL] [Abstract][Full Text] [Related]
4. [Characterization of S1' subsite specificity of Thermoactinomyces vulgaris carboxypeptidase T by site-directed mutagenesis].
Trachuk LA; Bushueva AM; Shevelev AB; Novgorodova SA; Akparov VKh; Chestukhina GG
Vopr Med Khim; 2002; 48(6):577-85. PubMed ID: 12698557
[TBL] [Abstract][Full Text] [Related]
5. Leu254 residue and calcium ions as new structural determinants of carboxypeptidase T substrate specificity.
Grishin AM; Akparov VKh; Chestukhina GG
Biochemistry (Mosc); 2008 Oct; 73(10):1140-5. PubMed ID: 18991561
[TBL] [Abstract][Full Text] [Related]
6. Mobile Loop in the Active Site of Metallocarboxypeptidases as an Underestimated Determinant of Substrate Specificity.
Akparov VK; Timofeev VI; Khaliullin IG; Konstantinova GE; Kuranova IP; Rakitina TV; Švedas VK
Biochemistry (Mosc); 2018 Dec; 83(12):1594-1602. PubMed ID: 30878033
[TBL] [Abstract][Full Text] [Related]
7. Structural insights into the broad substrate specificity of carboxypeptidase T from Thermoactinomyces vulgaris.
Akparov VKh; Timofeev VI; Khaliullin IG; Švedas V; Chestukhina GG; Kuranova IP
FEBS J; 2015 Apr; 282(7):1214-24. PubMed ID: 25619204
[TBL] [Abstract][Full Text] [Related]
8. Molecular cloning and primary structure of Thermoactinomyces vulgaris carboxypeptidase T. A metalloenzyme endowed with dual substrate specificity.
Smulevitch SV; Osterman AL; Galperina OV; Matz MV; Zagnitko OP; Kadyrov RM; Tsaplina IA; Grishin NV; Chestukhina GG; Stepanov VM
FEBS Lett; 1991 Oct; 291(1):75-8. PubMed ID: 1936254
[TBL] [Abstract][Full Text] [Related]
9. Three-dimensional structure of carboxypeptidase T from Thermoactinomyces vulgaris in complex with N-BOC-L-leucine.
Timofeev VI; Kuznetsov SA; Akparov VKh; Chestukhina GG; Kuranova IP
Biochemistry (Mosc); 2013 Mar; 78(3):252-9. PubMed ID: 23586718
[TBL] [Abstract][Full Text] [Related]
10. Primary structure of carboxypeptidase T: delineation of functionally relevant features in Zn-carboxypeptidase family.
Osterman AL; Grishin NV; Smulevitch SV; Matz MV; Zagnitko OP; Revina LP; Stepanov VM
J Protein Chem; 1992 Oct; 11(5):561-70. PubMed ID: 1449602
[TBL] [Abstract][Full Text] [Related]
11. Structure of the microbial carboxypeptidase T complexed with the transition state analog N-sulfamoyl-l-lysine.
Akparov VK; Konstantinova GE; Timofeev VI; Khaliullin IG; Kuranova IP
Biophys Chem; 2021 Mar; 270():106535. PubMed ID: 33412495
[TBL] [Abstract][Full Text] [Related]
12. The nature of the ligand's side chain interacting with the S1'-subsite of metallocarboxypeptidase T (from Thermoactinomyces vulgaris) determines the geometry of the tetrahedral transition complex.
Akparov VK; Timofeev VI; Konstantinova GE; Khaliullin IG; Kuranova IP; Rakitina TV; Švedas V
PLoS One; 2019; 14(12):e0226636. PubMed ID: 31887148
[TBL] [Abstract][Full Text] [Related]
13. [Carboxypeptidase T--intracellular carboxypeptidase of Thermoactinomycetes--a distant analog of animal carboxypeptidase].
Osterman AL; Stepanov VM; Rudenskaia GN; Khodova OM; Tsaplina IA
Biokhimiia; 1984 Feb; 49(2):292-301. PubMed ID: 6424730
[TBL] [Abstract][Full Text] [Related]
14. Crystal structure of carboxypeptidase T from Thermoactinomyces vulgaris.
Teplyakov A; Polyakov K; Obmolova G; Strokopytov B; Kuranova I; Osterman A; Grishin N; Smulevitch S; Zagnitko O; Galperina O
Eur J Biochem; 1992 Sep; 208(2):281-8. PubMed ID: 1521526
[TBL] [Abstract][Full Text] [Related]
15. Structure of the carboxypeptidase B complex with N-sulfamoyl-L-phenylalanine - a transition state analog of non-specific substrate.
Akparov V; Timofeev V; Khaliullin I; Švedas V; Kuranova I
J Biomol Struct Dyn; 2018 Mar; 36(4):956-965. PubMed ID: 28274181
[TBL] [Abstract][Full Text] [Related]
16. In vitro refolding of carboxypeptidase T precursor from Thermoactinomyces vulgaris obtained in Escherichia coli as cytoplasmic inclusion bodies.
Trachuk L; Letarov A; Kudelina IA; Yusupova MP; Chestukhina GG
Protein Expr Purif; 2005 Mar; 40(1):51-9. PubMed ID: 15721771
[TBL] [Abstract][Full Text] [Related]
17. Expression of the carboxypeptidase T gene from Thermoactinomyces vulgaris in stable protoplast type L-forms of Proteus mirabilis.
Bushueva AM; Shevelev AB; Gumpert J; Chestukhina GG; Serkina AV; Hoischen C; Matz MV; Kuryatova MV; Stepanov VM
FEMS Microbiol Lett; 1998 Feb; 159(2):145-50. PubMed ID: 9503606
[TBL] [Abstract][Full Text] [Related]
18. Comparative modeling of substrate binding in the S1' subsite of serine carboxypeptidases from yeast, wheat, and human.
Elsliger MA; Pshezhetsky AV; Vinogradova MV; Svedas VK; Potier M
Biochemistry; 1996 Nov; 35(47):14899-909. PubMed ID: 8942654
[TBL] [Abstract][Full Text] [Related]
19. The role of Tyr248 probed by mutant bovine carboxypeptidase A: insight into the catalytic mechanism of carboxypeptidase A.
Cho JH; Kim DH; Lee KJ; Kim DH; Choi KY
Biochemistry; 2001 Aug; 40(34):10197-203. PubMed ID: 11513597
[TBL] [Abstract][Full Text] [Related]
20. The specificity of carboxypeptidase Y may be altered by changing the hydrophobicity of the S'1 binding pocket.
Sørensen SB; Breddam K
Protein Sci; 1997 Oct; 6(10):2227-32. PubMed ID: 9336845
[TBL] [Abstract][Full Text] [Related]
[Next] [New Search]