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Volumn 1854, Issue 9, 2015, Pages 1167-1174

Chemistry and diversity of pyridoxal-5′-phosphate dependent enzymes

Author keywords

Acid base catalysis; Pyridoxal 5 phosphate; Reaction mechanism; Steady state kinetics; Stopped flow kinetics; Substrate strain

Indexed keywords

ALANINE; AMINOTRANSFERASE; CYTIDINE DEAMINASE; DIMER; HISTIDINE; KYNURENINASE; LYSINE; NITROGEN; PHENYLALANINE; PYRIDINE; PYRIDOXAL 5 PHOSPHATE; PYRIMIDINE DERIVATIVE; S ETHYLCYSTEINE; SERINE; TRYPTOPHAN; TYROSINE; TYROSINE PHENOL LYASE; HYDROLASE;

EID: 84937638704     PISSN: 15709639     EISSN: 18781454     Source Type: Journal    
DOI: 10.1016/j.bbapap.2014.12.028     Document Type: Review
Times cited : (64)

References (29)
  • 1
    • 70349753296 scopus 로고    scopus 로고
    • The B6 database: a tool for the description and classification of vitamin B6-dependent enzymatic activities and of the corresponding protein families
    • R. Percudani, and A. Peracchi The B6 database: a tool for the description and classification of vitamin B6-dependent enzymatic activities and of the corresponding protein families BMC Bioinformatics 10 2009 273
    • (2009) BMC Bioinformatics , vol.10 , pp. 273
    • Percudani, R.1    Peracchi, A.2
  • 2
    • 0013902457 scopus 로고
    • Conformation and reaction specificity in pyridoxal phosphate enzymes
    • H.C. Dunathan Conformation and reaction specificity in pyridoxal phosphate enzymes Proc. Natl. Acad. Sci. U. S. A. 55 1966 712 716
    • (1966) Proc. Natl. Acad. Sci. U. S. A. , vol.55 , pp. 712-716
    • Dunathan, H.C.1
  • 4
    • 0029092235 scopus 로고
    • Pulsed electron paramagnetic resonance studies of the lysine 2,3-aminomutase substrate radical: evidence for participation of pyridoxal 5′-phosphate in a radical rearrangement
    • M.D. Ballinger, P.A. Frey, G.H. Reed, and R. LoBrutto Pulsed electron paramagnetic resonance studies of the lysine 2,3-aminomutase substrate radical: evidence for participation of pyridoxal 5′-phosphate in a radical rearrangement Biochemistry 34 1995 10086 10093
    • (1995) Biochemistry , vol.34 , pp. 10086-10093
    • Ballinger, M.D.1    Frey, P.A.2    Reed, G.H.3    Lobrutto, R.4
  • 5
    • 0033649909 scopus 로고    scopus 로고
    • The molecular evolution of pyridoxal-5′-phosphate-dependent enzymes
    • P.K. Mehta, and P. Christen The molecular evolution of pyridoxal-5′-phosphate-dependent enzymes Adv. Enzymol. Relat. Areas Mol. Biol. 1998 129 184
    • (1998) Adv. Enzymol. Relat. Areas Mol. Biol. , pp. 129-184
    • Mehta, P.K.1    Christen, P.2
  • 6
    • 0018657638 scopus 로고
    • Kynureninases: enzymological properties and regulation mechanism
    • K. Soda, and K. Tanizawa Kynureninases: enzymological properties and regulation mechanism Adv. Enzymol. Relat. Areas Mol. Biol. 49 1979 1 40
    • (1979) Adv. Enzymol. Relat. Areas Mol. Biol. , vol.49 , pp. 1-40
    • Soda, K.1    Tanizawa, K.2
  • 7
    • 0021216801 scopus 로고
    • Mechanism-based inactivation of bacterial kynureninase by beta-substituted amino acids
    • G.M. Kishore Mechanism-based inactivation of bacterial kynureninase by beta-substituted amino acids J. Biol. Chem. 259 1984 10669 10674
    • (1984) J. Biol. Chem. , vol.259 , pp. 10669-10674
    • Kishore, G.M.1
  • 8
    • 0022363122 scopus 로고
    • Isolation and characterization of a rat liver enzyme with both cysteine conjugate beta-lyase and kynureninase activity
    • J.L. Stevens Isolation and characterization of a rat liver enzyme with both cysteine conjugate beta-lyase and kynureninase activity J. Biol. Chem. 260 1985 7945 7950
    • (1985) J. Biol. Chem. , vol.260 , pp. 7945-7950
    • Stevens, J.L.1
  • 9
    • 0027535572 scopus 로고
    • Homology of pyridoxal-5′-phosphate-dependent aminotransferases with the cobC (cobalamin synthesis), nifS (nitrogen fixation), pabC (p-aminobenzoate synthesis) and malY (abolishing endogenous induction of the maltose system) gene products
    • P.K. Mehta, and P. Christen Homology of pyridoxal-5′-phosphate-dependent aminotransferases with the cobC (cobalamin synthesis), nifS (nitrogen fixation), pabC (p-aminobenzoate synthesis) and malY (abolishing endogenous induction of the maltose system) gene products Eur. J. Biochem. 211 1993 373 376
    • (1993) Eur. J. Biochem. , vol.211 , pp. 373-376
    • Mehta, P.K.1    Christen, P.2
  • 10
    • 0842304745 scopus 로고    scopus 로고
    • Three-dimensional structure of kynureninase from Pseudomonas fluorescens
    • C. Momany, V. Levdikov, L. Blagova, S. Lima, and R.S. Phillips Three-dimensional structure of kynureninase from Pseudomonas fluorescens Biochemistry 43 2004 1193 1203
    • (2004) Biochemistry , vol.43 , pp. 1193-1203
    • Momany, C.1    Levdikov, V.2    Blagova, L.3    Lima, S.4    Phillips, R.S.5
  • 12
    • 60549096522 scopus 로고    scopus 로고
    • Crystal structure of the homo sapiens kynureninase-3-hydroxyhippuric acid inhibitor complex: insights into the molecular basis of kynureninase substrate specificity
    • S. Lima, S. Kumar, V. Gawandi, C. Momany, and R.S. Phillips Crystal structure of the homo sapiens kynureninase-3-hydroxyhippuric acid inhibitor complex: insights into the molecular basis of kynureninase substrate specificity J. Med. Chem. 52 2008 389 396
    • (2008) J. Med. Chem. , vol.52 , pp. 389-396
    • Lima, S.1    Kumar, S.2    Gawandi, V.3    Momany, C.4    Phillips, R.S.5
  • 13
    • 0036882394 scopus 로고    scopus 로고
    • Serine protease mechanism and specificity
    • L. Hedstrom Serine protease mechanism and specificity Chem. Rev. 102 2002 4501 4524
    • (2002) Chem. Rev. , vol.102 , pp. 4501-4524
    • Hedstrom, L.1
  • 14
    • 84894260039 scopus 로고    scopus 로고
    • The phosphate of pyridoxal-5′-phosphate is an acid/base catalyst in the mechanism of Pseudomonas fluorescens kynureninase
    • R.S. Phillips, I. Scott, R. Paulose, A. Patel, and T.C. Barron The phosphate of pyridoxal-5′-phosphate is an acid/base catalyst in the mechanism of Pseudomonas fluorescens kynureninase FEBS J. 281 2014 1100 1109
    • (2014) FEBS J. , vol.281 , pp. 1100-1109
    • Phillips, R.S.1    Scott, I.2    Paulose, R.3    Patel, A.4    Barron, T.C.5
  • 15
    • 1542743742 scopus 로고    scopus 로고
    • Reaction of Pseudomonas fluorescens kynureninase with β-benzoyl-l-alanine: detection of a new reaction intermediate and a change in rate-determining step
    • V.B. Gawandi, D. Liskey, S. Lima, and R.S. Phillips Reaction of Pseudomonas fluorescens kynureninase with β-benzoyl-l-alanine: detection of a new reaction intermediate and a change in rate-determining step Biochemistry 43 2004 3230 3237
    • (2004) Biochemistry , vol.43 , pp. 3230-3237
    • Gawandi, V.B.1    Liskey, D.2    Lima, S.3    Phillips, R.S.4
  • 16
    • 77956396927 scopus 로고    scopus 로고
    • Substituent effects on the reaction of β-benzoylalanines with Pseudomonas fluorescens kynureninase
    • S. Kumar, V.B. Gawandi, N. Capito, and R.S. Phillips Substituent effects on the reaction of β-benzoylalanines with Pseudomonas fluorescens kynureninase Biochemistry 49 2010 7913 7919
    • (2010) Biochemistry , vol.49 , pp. 7913-7919
    • Kumar, S.1    Gawandi, V.B.2    Capito, N.3    Phillips, R.S.4
  • 17
    • 0032477717 scopus 로고    scopus 로고
    • The catalytic mechanism of kynureninase from Pseudomonas fluorescens: insights from the effects of pH and isotopic substitution on steady-state and pre-steady-state kinetics
    • S.V. Koushik, J.A. Moore, B. Sundararaju, and R.S. Phillips The catalytic mechanism of kynureninase from Pseudomonas fluorescens: insights from the effects of pH and isotopic substitution on steady-state and pre-steady-state kinetics Biochemistry 37 1998 1376 1382
    • (1998) Biochemistry , vol.37 , pp. 1376-1382
    • Koushik, S.V.1    Moore, J.A.2    Sundararaju, B.3    Phillips, R.S.4
  • 18
    • 0032537603 scopus 로고    scopus 로고
    • The catalytic mechanism of kynureninase from Pseudomonas fluorescens: evidence for transient quinonoid and ketimine intermediates from rapid-scanning stopped-flow spectrophotometry
    • R.S. Phillips, B. Sundararaju, and S.V. Koushik The catalytic mechanism of kynureninase from Pseudomonas fluorescens: evidence for transient quinonoid and ketimine intermediates from rapid-scanning stopped-flow spectrophotometry Biochemistry 37 1998 8783 8789
    • (1998) Biochemistry , vol.37 , pp. 8783-8789
    • Phillips, R.S.1    Sundararaju, B.2    Koushik, S.V.3
  • 19
    • 0000899186 scopus 로고
    • Stereochemistry and mechanism of aldol reactions catalyzed by kynureninase
    • R.S. Phillips, and R.K. Dua Stereochemistry and mechanism of aldol reactions catalyzed by kynureninase J. Am. Chem. Soc. 113 1991 7385 7388
    • (1991) J. Am. Chem. Soc. , vol.113 , pp. 7385-7388
    • Phillips, R.S.1    Dua, R.K.2
  • 20
    • 0030982177 scopus 로고    scopus 로고
    • The crystal structure of Citrobacter freundii tyrosine phenol-lyase complexed with 3-(4′-hydroxyphenyl)propionic acid, together with site-directed mutagenesis and kinetic analysis, demonstrates that arginine-381 is required for substrate specificity
    • B. Sundararaju, A.A. Antson, R.S. Phillips, T.V. Demidkina, M.V. Barbolina, P. Gollnick, G.G. Dodson, and K.S. Wilson The crystal structure of Citrobacter freundii tyrosine phenol-lyase complexed with 3-(4′-hydroxyphenyl)propionic acid, together with site-directed mutagenesis and kinetic analysis, demonstrates that arginine-381 is required for substrate specificity Biochemistry 36 1997 6502 6510
    • (1997) Biochemistry , vol.36 , pp. 6502-6510
    • Sundararaju, B.1    Antson, A.A.2    Phillips, R.S.3    Demidkina, T.V.4    Barbolina, M.V.5    Gollnick, P.6    Dodson, G.G.7    Wilson, K.S.8
  • 21
    • 0029080978 scopus 로고
    • Site-directed mutagenesis of tyrosine-71 to phenylalanine in Citrobacter freundii tyrosine phenol-lyase: evidence for dual roles of tyrosine-71 as a general acid catalyst in the reaction mechanism and in cofactor binding
    • H.Y. Chen, T.V. Demidkina, and R.S. Phillips Site-directed mutagenesis of tyrosine-71 to phenylalanine in Citrobacter freundii tyrosine phenol-lyase: evidence for dual roles of tyrosine-71 as a general acid catalyst in the reaction mechanism and in cofactor binding Biochemistry 34 1995 12276 12283
    • (1995) Biochemistry , vol.34 , pp. 12276-12283
    • Chen, H.Y.1    Demidkina, T.V.2    Phillips, R.S.3
  • 22
    • 0036565775 scopus 로고    scopus 로고
    • Threonine-124 and phenylalanine-448 in Citrobacter freundii tyrosine phenol-lyase are necessary for activity with l-tyrosine
    • T. Demidkina, M. Barbolina, N. Faleev, B. Sundararaju, P. Gollnick, and R.S. Phillips Threonine-124 and phenylalanine-448 in Citrobacter freundii tyrosine phenol-lyase are necessary for activity with l-tyrosine Biochem. J. 363 2002 745 752
    • (2002) Biochem. J. , vol.363 , pp. 745-752
    • Demidkina, T.1    Barbolina, M.2    Faleev, N.3    Sundararaju, B.4    Gollnick, P.5    Phillips, R.S.6
  • 23
    • 33747144080 scopus 로고    scopus 로고
    • Aminoacrylate intermediates in the reaction of Citrobacter freundii tyrosine phenol-lyase
    • R.S. Phillips, H.Y. Chen, and N.G. Faleev Aminoacrylate intermediates in the reaction of Citrobacter freundii tyrosine phenol-lyase Biochemistry 45 2006 9575 9583
    • (2006) Biochemistry , vol.45 , pp. 9575-9583
    • Phillips, R.S.1    Chen, H.Y.2    Faleev, N.G.3
  • 25
    • 80054730696 scopus 로고    scopus 로고
    • Crystallographic snapshots of tyrosine phenol-lyase show that substrate strain plays a role in C-C bond cleavage
    • D. Milic, T.V. Demidkina, N.G. Faleev, Robert S. Phillips, D. Matkovic-Calogovic, and A.A. Antson Crystallographic snapshots of tyrosine phenol-lyase show that substrate strain plays a role in C-C bond cleavage J. Am. Chem. Soc. 133 2011 16468 16476
    • (2011) J. Am. Chem. Soc. , vol.133 , pp. 16468-16476
    • Milic, D.1    Demidkina, T.V.2    Faleev, N.G.3    Phillips, R.S.4    Matkovic-Calogovic, D.5    Antson, A.A.6
  • 26
    • 84913532285 scopus 로고    scopus 로고
    • The role of substrate strain in the mechanism of the carbon-carbon lyases
    • R.S. Phillips, T.V. Demidkina, and N.G. Faleev The role of substrate strain in the mechanism of the carbon-carbon lyases Bioorg. Chem. 57 2015 198 205
    • (2015) Bioorg. Chem. , vol.57 , pp. 198-205
    • Phillips, R.S.1    Demidkina, T.V.2    Faleev, N.G.3
  • 28
    • 0030887895 scopus 로고    scopus 로고
    • The structure of the cytidine deaminase-product complex provides evidence for efficient proton transfer and ground-state destabilization
    • S. Xiang, S.A. Short, R. Wolfenden, and C.W. Carter Jr. The structure of the cytidine deaminase-product complex provides evidence for efficient proton transfer and ground-state destabilization Biochemistry 36 1997 4768 4774
    • (1997) Biochemistry , vol.36 , pp. 4768-4774
    • Xiang, S.1    Short, S.A.2    Wolfenden, R.3    Carter, C.W.4
  • 29
    • 84883156844 scopus 로고    scopus 로고
    • Sub-ångström-resolution crystallography reveals physical distortions that enhance reactivity of a covalent enzymatic intermediate
    • S. Lüdtke, P. Neumann, K.M. Erixon, F. Leeper, R. Kluger, R. Ficner, and K. Tittmann Sub-ångström-resolution crystallography reveals physical distortions that enhance reactivity of a covalent enzymatic intermediate Nat. Chem. 5 2013 762 767
    • (2013) Nat. Chem. , vol.5 , pp. 762-767
    • Lüdtke, S.1    Neumann, P.2    Erixon, K.M.3    Leeper, F.4    Kluger, R.5    Ficner, R.6    Tittmann, K.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.