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Volumn 6, Issue 6, 1996, Pages 790-797

The diverse world of coenzyme A binding proteins

Author keywords

[No Author keywords available]

Indexed keywords

3 HYDROXYACYL COENZYME A DEHYDROGENASE; ACETYL COENZYME A ACETYLTRANSFERASE; ACYL COENZYME A DEHYDROGENASE; CHLORAMPHENICOL ACETYLTRANSFERASE; CITRATE SYNTHASE; COENZYME A; ENOYL COENZYME A HYDRATASE; MERCAPTAMINE; METHYLMALONYL COENZYME A MUTASE; NUCLEIC ACID BINDING PROTEIN; PANTOTHENIC ACID; SUCCINYL COENZYME A SYNTHETASE;

EID: 0030444352     PISSN: 0959440X     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0959-440X(96)80009-1     Document Type: Article
Times cited : (71)

References (31)
  • 4
    • 0020483375 scopus 로고
    • Crystallographic refinement and atomic models of two different forms of citrate synthase at 2.7 and 1.7A resolution
    • Remington S, Wiegand G, Huber R: Crystallographic refinement and atomic models of two different forms of citrate synthase at 2.7 and 1.7A resolution. J Mol Biol 1982, 158:111-152
    • (1982) J Mol Biol , vol.158 , pp. 111-152
    • Remington, S.1    Wiegand, G.2    Huber, R.3
  • 7
    • 0023041821 scopus 로고
    • Prediction of the occurrence of the ADP-binding βαβ-fold in proteins, using an ammo acid sequence fingerprint
    • Wierenga RK, Terpstra P. Hol WGJ: Prediction of the occurrence of the ADP-binding βαβ-fold in proteins, using an ammo acid sequence fingerprint, J Mol Biol 1986, 187:1 01 -107
    • (1986) J Mol Biol , vol.187 , pp. 101-107
    • Wierenga, R.K.1    Terpstra, P.2    Hol, W.G.J.3
  • 8
    • 12944300317 scopus 로고
    • Binding of nucleotides by proteins
    • Schulz GE: Binding of nucleotides by proteins. Curr Opin Struct Srb/1992, 2:61-67.
    • (1992) Curr Opin Struct Srb , vol.2 , pp. 61-67
    • Schulz, G.E.1
  • 9
    • 0025048136 scopus 로고
    • The P-loop- A common motif in ATP- and GTP-binding proteins
    • Saraste M, Sibbald PR, Wittingholer A: The P-loop- a common motif in ATP- and GTP-binding proteins. Trends Biol Sc/1990, 15:430-434.
    • (1990) Trends Biol Sc , vol.15 , pp. 430-434
    • Saraste, M.1    Sibbald, P.R.2    Wittingholer, A.3
  • 10
    • 0023516725 scopus 로고
    • Structure of L-3-hydroxyacyl-coenzyrne a dehydrogenasepreliminary chain tracing at 2.8 a resolution
    • Birktoft JJ, Holden HM, Hamlin R, Xuong NH, Banaszak U Structure of L-3-hydroxyacyl-coenzyrne A dehydrogenase: preliminary chain tracing at 2.8 A resolution. Pmc Wart Acacl Sei USA 1987 84:8262-8266,
    • (1987) Pmc Wart Acacl Sei USA , vol.84 , pp. 8262-8266
    • Birktoft, J.J.1    Holden, H.M.2    Hamlin, R.3    Xuong, N.H.4    Banaszak, U.5
  • 13
    • 0028174351 scopus 로고
    • The 2.3 a crystal structure of peroxisomal 3-ketoacyl-CoA thiolase of Saccharomyces cerevisiaea fivelayered ncxa structure constructed from two core domains of identical topology
    • 3. Mathieu M, Zeelen JR Pauptit RA, Erdmann R, Kunau W-H, Wierenga RK: The 2.3 A crystal structure of peroxisomal 3-ketoacyl-CoA thiolase of Saccharomyces cerevisiae: a fivelayered ncxa structure constructed from two core domains of identical topology. Structure 1994, 2:797-808.
    • (1994) Structure , vol.2 , pp. 797-808
    • Mathieu, M.1    Zeelen, J.R.2    Pauptit, R.A.3    Erdmann, R.4    Kunau, W.-H.5    Wierenga, R.K.6
  • 14
    • 0029066497 scopus 로고
    • Crystal structure of Pseudomonas mevalonii HMG-CoA reductase at S.OAngstrom resolution
    • Lawrence CM, Rodwell VW, Staulfacher CV: Crystal structure of Pseudomonas mevalonii HMG-CoA reductase at S.OAngstrom resolution. Science 1995, 266:1758-1762. The 3.0 A structure of HMG-CoA dehydrogenase is described. Crystallographies binding studies reveal the binding sites of NAD and 3-hydroxy-3-methylglutaryl CoA.
    • (1995) Science , vol.266 , pp. 1758-1762
    • Lawrence, C.M.1    Rodwell, V.W.2    Staulfacher, C.V.3
  • 15
    • 0029061966 scopus 로고
    • The Escherichla coli malonyl-CoAacyl carrier protein transacylase at 1.5 a resolution
    • Serre L, Verbree EC, Dauter Z, Stuit]e AR, Derewenda ZS. The Escherichla coli malonyl-CoA: acyl carrier protein transacylase at 1.5 A resolution. J Biol Chem 1995, 270 1 2961-12964. E. coll malonyl CoA acetyl carrier protein transacylass is important for the synthesis of fatty acids. It catalyzes the transfer ol a malony! moiety from CoA to the phosphopantetheine arm of the acyl carrier protein.
    • (1995) J Biol Chem , vol.270 , pp. 12961-12964
    • Serre, L.1    Verbree, E.C.2    Dauter, Z.3    Stuite, A.R.4    Derewenda, Z.S.5
  • 16
    • 0030037645 scopus 로고    scopus 로고
    • Structure of 4-chlorobenzoylCoA dehalogenase determined to 1.8 a resolutionan enzyme catalyst generated via adaptive mutation
    • 6. Benning MM, Tylor KL, Liu R-O., Yang G, Xiang H, Wesenberg G, Ounauway-Mariano D, Halden HM: Structure of 4-chlorobenzoylCoA dehalogenase determined to 1.8 A resolution: an enzyme catalyst generated via adaptive mutation. Biochemistry 1996, 35:8103-8109. The fold of 4-chlorobenzoyl-CoA dehalogenase is the same as the fold of enoyl-CoA hydratase. The structure, solved in the presence of 4-nydroxyben?oyl CoA, gives new insight into the catalytic mechanism of dehalogenase.
    • (1996) Biochemistry , vol.35 , pp. 8103-8109
    • Benning, M.M.1    Tylor, K.L.2    Liu, R.-O.3    Yang, G.4    Xiang, H.5    Wesenberg, G.6    Ounauway-Mariano, D.7    Halden, H.M.8
  • 17
    • 0025785846 scopus 로고
    • Crystal structure of an op_en conformation of citrate synthase from chicken heart at 2.8A resolution
    • 7. Liao D-l, Karpusas M, Remington J: Crystal structure of an op_en conformation of citrate synthase from chicken heart at 2.8A resolution. Biochemistry 1991, 30:5031-6036.
    • (1991) Biochemistry , vol.30 , pp. 5031-6036
    • D-l, L.1    Karpusas, M.2    Remington, J.3
  • 20
    • 0027285476 scopus 로고
    • Crystallographic analysis of substrate binding and catalysis in dihydrolipoyl transacetylase (E2p)
    • Mattevi A, Obmolova G, Kalk KH, Teplyakov A, Hol WGJ: Crystallographic analysis of substrate binding and catalysis in dihydrolipoyl transacetylase (E2p). Biochemistry 1993, 32:3887-3901.
    • (1993) Biochemistry , vol.32 , pp. 3887-3901
    • Mattevi, A.1    Obmolova, G.2    Kalk, K.H.3    Teplyakov, A.4    Hol, W.G.J.5
  • 21
    • 0027304244 scopus 로고
    • Crystal structures of mediumchain acyl-CoA dehydrogenase from pig mitochondria with and without substrate
    • Kirn J-JP, Wang M, Paschke R: Crystal structures of mediumchain acyl-CoA dehydrogenase from pig mitochondria with and without substrate. Biochemistry 1993, 90:7523-7527.
    • (1993) Biochemistry , vol.90 , pp. 7523-7527
    • Kirn, J.-J.P.1    Wang, M.2    Paschke, R.3
  • 22
    • 0028905236 scopus 로고
    • Threedimensional structure of butyryl-CoA dehydrogenase from Megasphaera elsdenii
    • Djordjevic S, Pace CP, Stankovich MT, Kim J-JP: Threedimensional structure of butyryl-CoA dehydrogenase from Megasphaera elsdenii. Biochemistry 1995, 34:2163-2171. This paper describes the structure of bacteria! butyryl CoA dehydrogenase, completed with acetoacetyl-CoA. The fold is similar to thai of the mammalian medium chain acyl-CoA dehydrogenase. Differences in 1ha fatly acid binding packet correlate with differences in chain length specificity.
    • (1995) Biochemistry , vol.34 , pp. 2163-2171
    • Djordjevic, S.1    Pace, C.P.2    Stankovich, M.T.3    Kim, J.-J.P.4
  • 23
    • 0001590330 scopus 로고
    • The TIM barrelthe most frequently occurring folding motif in proteins
    • Brändén C-I: The TIM barrel: the most frequently occurring folding motif in proteins. Curr Opin Struct Biol 1991, 1:978-983.
    • (1991) Curr Opin Struct Biol , vol.1 , pp. 978-983
    • Brändén, C.-I.1
  • 24
  • 27
    • 0028060573 scopus 로고
    • Engineering for redesign
    • Hedstrom L: Engineering for redesign. Curr Opin Struct Bio! 1994, 4:608-611.
    • (1994) Curr Opin Struct Bio! , vol.4 , pp. 608-611
    • Hedstrom, L.1
  • 28
    • 0028276977 scopus 로고
    • The crystal structure of succinyl-CoA synthetase from Escherichia cell at 2.5A resolution
    • Wolodko WT, Fraser ME, James MNG, Bridgers WA: The crystal structure of succinyl-CoA synthetase from Escherichia cell at 2.5A resolution. J Btol Chem 1994, 269:10083-10890.
    • (1994) J Btol Chem , vol.269 , pp. 10083-10890
    • Wolodko, W.T.1    Fraser, M.E.2    James, M.N.G.3    Bridgers, W.A.4
  • 29
    • 0030584657 scopus 로고    scopus 로고
    • How coenzyme B12 radicals are generatedthe crystal structure of m ethyl m a Ion y iCoA mutase at 2A resolution
    • Mancia F, Keep NH, Nakagawa A, Leadlay PR McSweeney S, Rasmussen B, Bosecke R Dial O, Evans PR: How coenzyme B12 radicals are generated: the crystal structure of m ethyl m a Ion y iCoA mutase at 2A resolution. Structure 1 996, 4:339-350, A beautiful description of the structure of this oe-heterodrmer (150 kDa), complexee! with coenzyme B12 and desulpho-CoA The structure gives insight into coenzyme B12 dependent catalysis.
    • Structure , vol.1 , pp. 339-350
    • Mancia, F.1    Keep, N.H.2    Nakagawa, A.3    Leadlay, P.R.4    McSweeney, S.5    Rasmussen, B.6    Dial O, B.R.7    Evans, P.R.8
  • 30
    • 0029791410 scopus 로고    scopus 로고
    • Crystal structure of enoyl-CoA hydratase at 2.5 Aresolution a spiral fold defines the CoA binding site
    • Engel ChK, Mathieu M, Zeelen JPh, Hillurien JK, Wjerenga RK: Crystal structure of enoyl-CoA hydratase at 2.5 Aresolution: a spiral fold defines the CoA binding site. E M BO j 1996, 15:5135-5145. The crystal structure of enoyl-CoA hydratase complexed with acelyl-CoA visualizes the mode of binding of CoA to a spiral fold. The active-site architecture shows the importance of two glutamates for catalysis.
    • (1996) E M BO J , vol.15 , pp. 5135-5145
    • Engel, C.1    Mathieu, M.2    Zeelen, J.3    Hillurien, J.K.4
  • 31
    • 0027289149 scopus 로고
    • Three-dimensional structure of the complex between acyl-coenzyme a binding protein and palmttoyl-coenzyme a
    • Kragelund BB, Andersen VK, Madsen JC, Knudsen J, Poulsen FM: Three-dimensional structure of the complex between acyl-coenzyme A binding protein and palmttoyl-coenzyme A. J Mo! Biol 1993, 230:1260-1 277.
    • (1993) J Mo! Biol , vol.230 , pp. 1260-1277
    • Kragelund, B.B.1    Andersen, V.K.2    Madsen, J.C.3    Knudsen, J.4    Poulsen, F.M.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.