-
2
-
-
85030302950
-
-
J.E. Baldwin, C.J. Schofield, Page M.I. London: Blackie. The Chemistry of β-Lactams
-
Baldwin JE, Schofield CJ, Page MI. The biosynthesis of β lactams. 1:1992;Blackie, London. The Chemistry of β-Lactams.
-
(1992)
The Biosynthesis of β Lactams
, vol.1
-
-
-
4
-
-
0023243945
-
δ(Lα-aminoadipyl) L-cysteinyl-Dvaline synthetase (ACV synthetase) - multifunctional enzyme with broad substrate-specificity for the synthesis of penicillin and cephalosporin precursors
-
Banko G, Wolfe S, Demain AL. δ(Lα-aminoadipyl) L-cysteinyl-Dvaline synthetase (ACV synthetase) - multifunctional enzyme with broad substrate-specificity for the synthesis of penicillin and cephalosporin precursors. J Am Chem Soc. 109:1987;2858-2866.
-
(1987)
J Am Chem Soc
, vol.109
, pp. 2858-2866
-
-
Banko, G.1
Wolfe, S.2
Demain, A.L.3
-
5
-
-
0024590380
-
δ-(L-α-aminoadipyl)-L-cysteinyl-D-valine synthetase from Aspergillus-nidulans - The 1st enzyme in penicillin biosynthesis is a multifunctional peptide sythetase
-
Van Liempt H, Von Döhren H. δ-(L-α-aminoadipyl)-L-cysteinyl-D-valine synthetase from Aspergillus-nidulans - the 1st enzyme in penicillin biosynthesis is a multifunctional peptide sythetase. J Biol Chem. 264:1989;3860-3864.
-
(1989)
J Biol Chem
, vol.264
, pp. 3860-3864
-
-
Van Liempt, H.1
Von Döhren, H.2
-
6
-
-
0004251649
-
-
H. Kleinkauf, Von Döhren H. Berlin: deGruyter
-
Kleinkauf H, Von Döhren H. Biochemistry of peptide antibiotics. 1990;deGruyter, Berlin.
-
(1990)
Biochemistry of Peptide Antibiotics
-
-
-
7
-
-
0029921158
-
A nonribosomal system of peptide biosynthesis
-
of special interest. An excellent overview of current biochemical research on peptide synthetases.
-
Kleinkauf H, Von Döhren H. A nonribosomal system of peptide biosynthesis. of special interest Eur J Biochem. 236:1996;35-351 An excellent overview of current biochemical research on peptide synthetases.
-
(1996)
Eur J Biochem
, vol.236
, pp. 35-351
-
-
Kleinkauf, H.1
Von Döhren, H.2
-
8
-
-
0031060707
-
Thiol template peptide synthesis sytems in bacteria and fungi
-
of special interest. Complements [7] from a more microbiological point of view.
-
Zocher R, Keller U. Thiol template peptide synthesis sytems in bacteria and fungi. of special interest Adv Microbial Physiol. 38:1997;85-131 Complements [7] from a more microbiological point of view.
-
(1997)
Adv Microbial Physiol
, vol.38
, pp. 85-131
-
-
Zocher, R.1
Keller, U.2
-
9
-
-
0025895820
-
δ-(L-α-aminoadipyl)-L-cysteinyl-D-valine synthetase from Aspergillus-nidulans - molecular characterization of the acva gene encoding the 1st enzyme of the penicillin biosynthetic-pathway
-
MacCabe AP, Van Liempt H, Palissa H, Unkles SE, Riach MBR, Pfiefer E, Von Döhren H, Kinghorn JR. δ-(L-α-aminoadipyl)-L-cysteinyl-D-valine synthetase from Aspergillus-nidulans - molecular characterization of the acva gene encoding the 1st enzyme of the penicillin biosynthetic-pathway. J Biol Chem. 266:1991;12646-12654.
-
(1991)
J Biol Chem
, vol.266
, pp. 12646-12654
-
-
MacCabe, A.P.1
Van Liempt, H.2
Palissa, H.3
Unkles, S.E.4
Riach, M.B.R.5
Pfiefer, E.6
Von Döhren, H.7
Kinghorn, J.R.8
-
10
-
-
0025904272
-
Characterization of the Cephalosporium acremonium pcbab gene encoding α-aminoadipylcysteinyl-valine synthetase, a large multidomain peptide synthetase - linkage to the pcbc gene as a cluster of early cephalosporing biosynthetic genes and evidence of multiple functional domains
-
Gutierrez S, Diez B, Montenegro E, Martin JF. Characterization of the Cephalosporium acremonium pcbab gene encoding α-aminoadipylcysteinyl-valine synthetase, a large multidomain peptide synthetase - linkage to the pcbc gene as a cluster of early cephalosporing biosynthetic genes and evidence of multiple functional domains. J Bacteriol. 173:1991;2354-2365.
-
(1991)
J Bacteriol
, vol.173
, pp. 2354-2365
-
-
Gutierrez, S.1
Diez, B.2
Montenegro, E.3
Martin, J.F.4
-
11
-
-
0025004152
-
The multifunctional peptide synthetase performing the 1st step of penicillin biosynthesis in Penicillium chrysogeneum is a 421, 073 Dalton protein similar to Bacillus brevis peptide antibiotic synthetases
-
Smith DJ, Earl AJ, Turner G. The multifunctional peptide synthetase performing the 1st step of penicillin biosynthesis in Penicillium chrysogeneum is a 421, 073 Dalton protein similar to Bacillus brevis peptide antibiotic synthetases. EMBO J. 1990;2743-2750.
-
(1990)
EMBO J
, pp. 2743-2750
-
-
Smith, D.J.1
Earl, A.J.2
Turner, G.3
-
12
-
-
0031215148
-
Protein templates for the biosynthesis of peptide antibiotics
-
of outstanding interest. This paper gives an overview of structural studies on firefly luciferase and gramicidin S synthetase within the context of sequence similarities and demonstrates the domain structure of peptide synthetases.
-
Marahiel MA. Protein templates for the biosynthesis of peptide antibiotics. of outstanding interest Chem Biol. 4:1997;561-567 This paper gives an overview of structural studies on firefly luciferase and gramicidin S synthetase within the context of sequence similarities and demonstrates the domain structure of peptide synthetases.
-
(1997)
Chem Biol
, vol.4
, pp. 561-567
-
-
Marahiel, M.A.1
-
13
-
-
0029034197
-
Rational design of peptide antibiotics by targeted replacement of bacterial and fungal domain
-
Stachelaus T, Schnieder A, Mahariel MA. Rational design of peptide antibiotics by targeted replacement of bacterial and fungal domain. Science. 269:1995;69-72.
-
(1995)
Science
, vol.269
, pp. 69-72
-
-
Stachelaus, T.1
Schnieder, A.2
Mahariel, M.A.3
-
14
-
-
0015209453
-
Attempts to map a process evolution of peptide biosynthesis
-
Lipmann F. Attempts to map a process evolution of peptide biosynthesis. Science. 173:1971;875-884.
-
(1971)
Science
, vol.173
, pp. 875-884
-
-
Lipmann, F.1
-
15
-
-
0028211466
-
Detection of 4′-phosphopantetheine at the thiester binding site for L-valine of gramicidins synthetase-2
-
Stein T, Vater J, Kruft V, Wittman-Liebold B, Franke P, Panico M, McDowell R, Morris HR. Detection of 4′-phosphopantetheine at the thiester binding site for L-valine of gramicidins synthetase-2. FEBS Letts. 340:1994;39-44.
-
(1994)
FEBS Letts
, vol.340
, pp. 39-44
-
-
Stein, T.1
Vater, J.2
Kruft, V.3
Wittman-Liebold, B.4
Franke, P.5
Panico, M.6
McDowell, R.7
Morris, H.R.8
-
16
-
-
0028964503
-
Gramicidin-S synthetase-1 (phenylalanine racemase), a prototype of amino-acid racemases containing the cofactor 4′-phosphopantetheine
-
Stein T, Kluge B, Vater J, Franke P, Otto A, Wittmannliebold B. Gramicidin-S synthetase-1 (phenylalanine racemase), a prototype of amino-acid racemases containing the cofactor 4′-phosphopantetheine. Biochemistry. 34:1995;4633-4642.
-
(1995)
Biochemistry
, vol.34
, pp. 4633-4642
-
-
Stein, T.1
Kluge, B.2
Vater, J.3
Franke, P.4
Otto, A.5
Wittmannliebold, B.6
-
17
-
-
0028985406
-
δ-L-(α-aminodipoyl)-L-cysteinyl-D-valine synthetase - The order of peptide-bond formation and timing of the epimerization reaction
-
Shiau CY, Baldwin JE, Byford MF, Sobey WJ, Schofield CJ. δ-L-(α-aminodipoyl)-L-cysteinyl-D-valine synthetase - the order of peptide-bond formation and timing of the epimerization reaction. FEBS Lett. 358:1995;97-100.
-
(1995)
FEBS Lett
, vol.358
, pp. 97-100
-
-
Shiau, C.Y.1
Baldwin, J.E.2
Byford, M.F.3
Sobey, W.J.4
Schofield, C.J.5
-
18
-
-
0028142411
-
Epimerization of the D-valine portion in the biosynthesis of actinomycin-D
-
Stindl A, Keller U. Epimerization of the D-valine portion in the biosynthesis of actinomycin-D. Biochemistry. 33:1994;9358-9364.
-
(1994)
Biochemistry
, vol.33
, pp. 9358-9364
-
-
Stindl, A.1
Keller, U.2
-
19
-
-
0030798913
-
L-δ-(α-aminoadipoyl)-L-cysteinyl-D-valine synthetase: Thioesterification is not obligatory for peptide bond formation
-
of special interest. The authors demonstrate that formation of a thioester bond is not essential for peptide synthetase catalyzed amide bond formation.
-
Shiau CY, Balwin JE, Byford MF, Aplin RT, Schofield CJ. L-δ-(α-aminoadipoyl)-L-cysteinyl-D-valine synthetase: thioesterification is not obligatory for peptide bond formation. of special interest Biochemistry. 35:1997;8798-9906 The authors demonstrate that formation of a thioester bond is not essential for peptide synthetase catalyzed amide bond formation.
-
(1997)
Biochemistry
, vol.35
, pp. 8798-9906
-
-
Shiau, C.Y.1
Balwin, J.E.2
Byford, M.F.3
Aplin, R.T.4
Schofield, C.J.5
-
20
-
-
0028971311
-
L-δ-(α-aminoadipoyl)-L-cysteinyl-D-valine synthetase - L-cysteinyl-D-valine a shunt product, and implications for the order of peptide-bond formation
-
Shiau CY, Baldwin JE, Byford MF, Schofield CJ. L-δ-(α-aminoadipoyl)-L-cysteinyl-D-valine synthetase - L-cysteinyl-D-valine a shunt product, and implications for the order of peptide-bond formation. FEBS Lett. 373:1995;303-306.
-
(1995)
FEBS Lett
, vol.373
, pp. 303-306
-
-
Shiau, C.Y.1
Baldwin, J.E.2
Byford, M.F.3
Schofield, C.J.4
-
21
-
-
0029048654
-
Characterization of tyrocidine synthetase-1 (TY1)-requirement of post -translational modification for peptide biosynthesis
-
Pfeifer E, Pavela-Vranic M, Von Döhren H, Kleinkauf H. Characterization of tyrocidine synthetase-1 (TY1)-requirement of post -translational modification for peptide biosynthesis. Biochemistry. 34:1995;7450-7459.
-
(1995)
Biochemistry
, vol.34
, pp. 7450-7459
-
-
Pfeifer, E.1
Pavela-Vranic, M.2
Von Döhren, H.3
Kleinkauf, H.4
-
22
-
-
0028882690
-
Cloning, overproduction, and characterization of the Escherichia coli holo-acyl carrier protein synthase
-
Lambalot RH, Walsh CT. Cloning, overproduction, and characterization of the Escherichia coli holo-acyl carrier protein synthase. J Biol Chem. 270:1995;24658-24661.
-
(1995)
J Biol Chem
, vol.270
, pp. 24658-24661
-
-
Lambalot, R.H.1
Walsh, C.T.2
-
23
-
-
0030294470
-
A new enzyme superfamily-the phosphopantetheinyl transferases
-
of special interest. Overview of the emerging phosphopantetheinyl transferase enzyme family that catalyse an essential post-translational modification of specific enzymes whose mechanism involves transfer of activated acyl groups.
-
Lambalot RH, Gehring AM, Flugel RS, Zuber P, Lacelle M, Marahiel MA, Reid R, Knosla C, Walsh CT. A new enzyme superfamily-the phosphopantetheinyl transferases. of special interest Chem Biol. 3:1996;923-936 Overview of the emerging phosphopantetheinyl transferase enzyme family that catalyse an essential post-translational modification of specific enzymes whose mechanism involves transfer of activated acyl groups.
-
(1996)
Chem Biol
, vol.3
, pp. 923-936
-
-
Lambalot, R.H.1
Gehring, A.M.2
Flugel, R.S.3
Zuber, P.4
Lacelle, M.5
Marahiel, M.A.6
Reid, R.7
Knosla, C.8
Walsh, C.T.9
-
25
-
-
0031105254
-
Expression of a functional non-ribosomal peptide synthetase module in Escherichia coli by coexpression with phosphopantetheinyl transferase
-
of outstanding interest. Demonstrates the post-translational phosphopantetheinylation of over-expressed synthetases is possible in a heterologous host if the appropriate phosphopantetheine transferase is co-expressed.
-
Ku J, Mirmira RG, Liu L, Santi DV. Expression of a functional non-ribosomal peptide synthetase module in Escherichia coli by coexpression with phosphopantetheinyl transferase. of outstanding interest Chem Biol. 4:1997;203-207 Demonstrates the post-translational phosphopantetheinylation of over-expressed synthetases is possible in a heterologous host if the appropriate phosphopantetheine transferase is co-expressed.
-
(1997)
Chem Biol
, vol.4
, pp. 203-207
-
-
Ku, J.1
Mirmira, R.G.2
Liu, L.3
Santi, D.V.4
-
26
-
-
0030584662
-
Crystal-structure of firefly luciferase throws light on a superfamily of adenylated-forming enzymes
-
of outstanding interest. The paper reports the first structure determination of an enzyme from the family of non-ribosomal adenylate-forming enzymes that includes the peptide synthetases.
-
Conti E, Franks NP, Brick P. Crystal-structure of firefly luciferase throws light on a superfamily of adenylated-forming enzymes. of outstanding interest Structure. 4:1996;287-298 The paper reports the first structure determination of an enzyme from the family of non-ribosomal adenylate-forming enzymes that includes the peptide synthetases.
-
(1996)
Structure
, vol.4
, pp. 287-298
-
-
Conti, E.1
Franks, N.P.2
Brick, P.3
-
27
-
-
0030756031
-
Structural basis for the activation of phenylalanine in the non-ribosomal biosynthesis of gramicidin A
-
of outstanding interest. Documents the first structure of an adenylate-forming module from a peptide synthetase.
-
Conti E, Stachellhaus T, Marahiel MA, Brick P. Structural basis for the activation of phenylalanine in the non-ribosomal biosynthesis of gramicidin A. of outstanding interest EMBO J. 16:1997;4174-4183 Documents the first structure of an adenylate-forming module from a peptide synthetase.
-
(1997)
EMBO J
, vol.16
, pp. 4174-4183
-
-
Conti, E.1
Stachellhaus, T.2
Marahiel, M.A.3
Brick, P.4
-
28
-
-
0039302669
-
Dioxygen activation by enzymes with mononuclear non-heme iron active sites
-
of special interest. The best current review on mononuclear non-haem iron oxygenases/oxidases.
-
Que L, Ho RYN. Dioxygen activation by enzymes with mononuclear non-heme iron active sites. of special interest Chem Rev. 96:1996;2607-2624 The best current review on mononuclear non-haem iron oxygenases/oxidases.
-
(1996)
Chem Rev
, vol.96
, pp. 2607-2624
-
-
Que, L.1
Ho, R.Y.N.2
-
29
-
-
0000239991
-
Dioxygen activation by enzymes containing binuclear non-heme iron clusters
-
of special interest. The best current review on dinuclear non-haem iron oxygenases/oxidases.
-
Wallar BJ, Lipscomb JD. Dioxygen activation by enzymes containing binuclear non-heme iron clusters. of special interest Chem Rev. 96:1996;2625-2657 The best current review on dinuclear non-haem iron oxygenases/oxidases.
-
(1996)
Chem Rev
, vol.96
, pp. 2625-2657
-
-
Wallar, B.J.1
Lipscomb, J.D.2
-
30
-
-
0029038392
-
Crystal structure of isopenicillin N synthase is first from a new structural family
-
Roach PL, Clifton IJ, Fülöp V, Harlos K, Barton GJ, Hajdu J, Andersson I, Schofield CJ, Baldwin JE. Crystal structure of isopenicillin N synthase is first from a new structural family. Nature. 7:1995;700-704.
-
(1995)
Nature
, vol.7
, pp. 700-704
-
-
Roach, P.L.1
Clifton, I.J.2
Fülöp, V.3
Harlos, K.4
Barton, G.J.5
Hajdu, J.6
Andersson, I.7
Schofield, C.J.8
Baldwin, J.E.9
-
31
-
-
0030947388
-
Structure of isopenicillin n synthase complexed to substrate and the mechanism of penicillin formation
-
of outstanding interest. This paper presents the first reported structure of a non-haem iron mono-oxygenase complexed to its substrate (and NO as a dioxygen analogue).
-
Roach PL, Clifton IJ, Shibata N, Hajdu J, Schofield CJ, Baldwin JE. Structure of isopenicillin n synthase complexed to substrate and the mechanism of penicillin formation. of outstanding interest Nature. 387:1997;827-830 This paper presents the first reported structure of a non-haem iron mono-oxygenase complexed to its substrate (and NO as a dioxygen analogue).
-
(1997)
Nature
, vol.387
, pp. 827-830
-
-
Roach, P.L.1
Clifton, I.J.2
Shibata, N.3
Hajdu, J.4
Schofield, C.J.5
Baldwin, J.E.6
-
32
-
-
0024296029
-
Structure and assembly of protocatechuate 3,4-dioxygenase
-
Ohlendorf DH, Liposcomb JD, Weber PC. Structure and assembly of protocatechuate 3,4-dioxygenase. Nature. 336:1988;403-405.
-
(1988)
Nature
, vol.336
, pp. 403-405
-
-
Ohlendorf, D.H.1
Liposcomb, J.D.2
Weber, P.C.3
-
33
-
-
0028067892
-
Structure of protocatechuate 3,4-dioxygenase from Pseudomonas-aeruginosa at 2.15 Å resolution
-
Ohlendorf DH, Orville AM, Lipscomb JD. Structure of protocatechuate 3,4-dioxygenase from Pseudomonas-aeruginosa at 2.15 Å resolution. J Mol Biol. 244:1994;586-608.
-
(1994)
J Mol Biol
, vol.244
, pp. 586-608
-
-
Ohlendorf, D.H.1
Orville, A.M.2
Lipscomb, J.D.3
-
34
-
-
0030008087
-
3-Dimensional structures of free-form and 2 substrate complexes of an extradiol ring-cleavage type dioxygenase, the bphc enzyme from Pseudomonas sp strain KKS102
-
of special interest. of outstanding interest. Together with [35], this work provides a detailed insight into the iron-binding site of the extradiol dioxygenases and is especially interesting in a comparison with IPNS. The structure determination was carried out under aerobic conditions [the enzyme contained inactive FE(III) rather than Fe(II) allowing the structure of enzyme-substrate complexes to be determined.
-
of special interest Senda T, Sugiyama K, Narita H, Yamamoto T, Kimbara K, Fukuda M, Satao M, Yano K, Mitsui Y. 3-Dimensional structures of free-form and 2 substrate complexes of an extradiol ring-cleavage type dioxygenase, the bphc enzyme from Pseudomonas sp strain KKS102. of outstanding interest J Mol Biol. 225:1996;735-752 Together with [35], this work provides a detailed insight into the iron-binding site of the extradiol dioxygenases and is especially interesting in a comparison with IPNS. The structure determination was carried out under aerobic conditions [the enzyme contained inactive FE(III) rather than Fe(II) allowing the structure of enzyme-substrate complexes to be determined.
-
(1996)
J Mol Biol
, vol.225
, pp. 735-752
-
-
Senda, T.1
Sugiyama, K.2
Narita, H.3
Yamamoto, T.4
Kimbara, K.5
Fukuda, M.6
Satao, M.7
Yano, K.8
Mitsui, Y.9
-
35
-
-
0028862027
-
Crystal-structure of the biphenyl-cleaving extradiol dioxygenase from a pcb-degrading Pseudomonad
-
of outstanding influence. of special interest. Description of an extradiol dioxygenase structure under anaerobic conditions. The observed coordination chemistry of the iron was very similar to that described in [34].
-
of outstanding influence Han S, Eltis LD, Timmis KN, Muchmore SW, Bolin JT. Crystal-structure of the biphenyl-cleaving extradiol dioxygenase from a pcb-degrading Pseudomonad. of special interest Science. 270:1995;976-980 Description of an extradiol dioxygenase structure under anaerobic conditions. The observed coordination chemistry of the iron was very similar to that described in [34].
-
(1995)
Science
, vol.270
, pp. 976-980
-
-
Han, S.1
Eltis, L.D.2
Timmis, K.N.3
Muchmore, S.W.4
Bolin, J.T.5
-
36
-
-
0027246677
-
The 3-dimensional structure of an arachidonic-acid 15-lipoxygenase
-
Boyington JC, Gaffney BJ, Amzel LM. The 3-dimensional structure of an arachidonic-acid 15-lipoxygenase. Science. 260:1993;1482-1486.
-
(1993)
Science
, vol.260
, pp. 1482-1486
-
-
Boyington, J.C.1
Gaffney, B.J.2
Amzel, L.M.3
-
37
-
-
0029740369
-
Crystal-structure of soybean lipoxygenase 1-1 at 1.4 angstrom resolution
-
of outstanding interest. High resolution structure of lipoxygenase provides detailed insights into its unique coordination chemistry.
-
Minor W, Steczko J, Stec B, Otwinowski Z, Bolin JT, Walter R, Axelrod B. Crystal-structure of soybean lipoxygenase 1-1 at 1.4 angstrom resolution. of outstanding interest Biochemistry. 35:1996;10687-10701 High resolution structure of lipoxygenase provides detailed insights into its unique coordination chemistry.
-
(1996)
Biochemistry
, vol.35
, pp. 10687-10701
-
-
Minor, W.1
Steczko, J.2
Stec, B.3
Otwinowski, Z.4
Bolin, J.T.5
Walter, R.6
Axelrod, B.7
-
39
-
-
0027280014
-
X-ray absorption studies of the ferrous active-site of isopenicillin-N synthase and related model complexes
-
Randall CR, Zang Y, True AE, Que J, Charnock JM, Garner CD, Fujishima Y, Schofield CJ, Baldwin JE. X-ray absorption studies of the ferrous active-site of isopenicillin-N synthase and related model complexes. Biochemistry. 32:1993;6664-6673.
-
(1993)
Biochemistry
, vol.32
, pp. 6664-6673
-
-
Randall, C.R.1
Zang, Y.2
True, A.E.3
Que, J.4
Charnock, J.M.5
Garner, C.D.6
Fujishima, Y.7
Schofield, C.J.8
Baldwin, J.E.9
-
40
-
-
0028906347
-
Crystallization and preliminary X-ray diffraction studies on recombinant isopenicillin-N synthase from Aspergillus nidulans
-
Roach PL, Schofield CJ, Baldwin JE, Clifton IJ, Hajdu J. Crystallization and preliminary X-ray diffraction studies on recombinant isopenicillin-N synthase from Aspergillus nidulans. Protein Sci. 4:1995;1007-1009.
-
(1995)
Protein Sci
, vol.4
, pp. 1007-1009
-
-
Roach, P.L.1
Schofield, C.J.2
Baldwin, J.E.3
Clifton, I.J.4
Hajdu, J.5
-
41
-
-
0030025142
-
Functional-analysis of conserved histidine-residues in Cephalosporium acremonium isopenicillin-N synthase by site-directed mutagenesis
-
Tan SH, Sim TS. Functional-analysis of conserved histidine-residues in Cephalosporium acremonium isopenicillin-N synthase by site-directed mutagenesis. J Biol Chem. 271:1996;889-894.
-
(1996)
J Biol Chem
, vol.271
, pp. 889-894
-
-
Tan, S.H.1
Sim, T.S.2
-
42
-
-
0030032150
-
Ferous active-site of isopenicillin N synthase - genetic and sequence-analysis of the endogenous ligands
-
Borovok L, Landman O, Kreisberg-Zakarin R, Ahaaronowitz Y, Cohen G. Ferous active-site of isopenicillin N synthase - genetic and sequence-analysis of the endogenous ligands. Biochemistry. 35:1996;1981-1987.
-
(1996)
Biochemistry
, vol.35
, pp. 1981-1987
-
-
Borovok, L.1
Landman, O.2
Kreisberg-Zakarin, R.3
Ahaaronowitz, Y.4
Cohen, G.5
-
43
-
-
0030964827
-
The glutamine ligand in the ferrous iron active site of isopenicillin n synthase of Streptomyces jumonjinensis is not essential for catalysis
-
Landman O, Borovok I, Aharonowitz Y, Cohen G. The glutamine ligand in the ferrous iron active site of isopenicillin n synthase of Streptomyces jumonjinensis is not essential for catalysis. FEBS Lett. 405:1997;172-174.
-
(1997)
FEBS Lett
, vol.405
, pp. 172-174
-
-
Landman, O.1
Borovok, I.2
Aharonowitz, Y.3
Cohen, G.4
-
44
-
-
0031004173
-
Glutamine-330 is not essential for activity in isopenicillin N synthase from Asergillus nidulans
-
Sami M, Brown TJN, Roach PL, Schofield CJ, Baldwin JE. Glutamine-330 is not essential for activity in isopenicillin N synthase from Asergillus nidulans. FEBS Lett. 405:1997;191-194.
-
(1997)
FEBS Lett
, vol.405
, pp. 191-194
-
-
Sami, M.1
Brown, T.J.N.2
Roach, P.L.3
Schofield, C.J.4
Baldwin, J.E.5
-
45
-
-
8044241575
-
Anaerobic crystallisation of an isopenicillin N synthase-Fe(II)-substrate complex demonstrated by X-ray studies
-
Roach PL, Clifton IJ, Hensengs CMH, Shibata N, Long AJ, Strange RW, Hasnain SS, Schofield CJ, Baldwin JE, Hajdu J. Anaerobic crystallisation of an isopenicillin N synthase-Fe(II)-substrate complex demonstrated by X-ray studies. Eur J Biochem. 242:1996;736-740.
-
(1996)
Eur J Biochem
, vol.242
, pp. 736-740
-
-
Roach, P.L.1
Clifton, I.J.2
Hensengs, C.M.H.3
Shibata, N.4
Long, A.J.5
Strange, R.W.6
Hasnain, S.S.7
Schofield, C.J.8
Baldwin, J.E.9
Hajdu, J.10
-
46
-
-
0001375191
-
Antisense gene that inhibits synthesis of the hormone ethylene in transgenic plants
-
Hamilton AJ, Lycett GW, Grierson D. Antisense gene that inhibits synthesis of the hormone ethylene in transgenic plants. Nature. 346:1990;284-287.
-
(1990)
Nature
, vol.346
, pp. 284-287
-
-
Hamilton, A.J.1
Lycett, G.W.2
Grierson, D.3
-
47
-
-
0030962028
-
Characterization of the iron- And 2- oxyglutarate-binding sites of human prolyl 4-hydroxylase
-
of special interest. An interesting mutagenesis-kinetic study on the active site of prolyl-4-hydroxylase is presented.
-
Myllyharju J, Kivirikko KI. Characterization of the iron- and 2- oxyglutarate-binding sites of human prolyl 4-hydroxylase. of special interest EMBO J. 16:1997;1173-1180 An interesting mutagenesis-kinetic study on the active site of prolyl-4-hydroxylase is presented.
-
(1997)
EMBO J
, vol.16
, pp. 1173-1180
-
-
Myllyharju, J.1
Kivirikko, K.I.2
-
48
-
-
0029805240
-
Analysis of bacterial carbapenem antibiotic production genes reveals a novel β-lactam biosynthesis pathway
-
of special interest. Sequencing of the carbapenam biosynthesis operon opens up the way for study of the individual biosynthetic enzymes and for attempts to optimise the fermentaion of carbapenem antibiotics, which are currently made by expensive total synthesis.
-
McGowan SJ, Sebaihia M, Porter LE, Stewart GSAB, William P, Bycroft BW, Salmond GPC. Analysis of bacterial carbapenem antibiotic production genes reveals a novel β-lactam biosynthesis pathway. of special interest Mol Microbiol. 22:1996;415-426 Sequencing of the carbapenam biosynthesis operon opens up the way for study of the individual biosynthetic enzymes and for attempts to optimise the fermentaion of carbapenem antibiotics, which are currently made by expensive total synthesis.
-
(1996)
Mol Microbiol
, vol.22
, pp. 415-426
-
-
McGowan, S.J.1
Sebaihia, M.2
Porter, L.E.3
Stewart, G.4
William, P.5
Bycroft, B.W.6
Salmond, G.P.C.7
-
49
-
-
0028964402
-
Expression and purification of 2 isozymes of clavaminate synthase and initial characterization of the iron-binding site - general error analysis in polymerase chain-reaction amplication
-
Busby RW, Chang MDT, Busby RC, Wimp J, Townsend CA. Expression and purification of 2 isozymes of clavaminate synthase and initial characterization of the iron-binding site - general error analysis in polymerase chain-reaction amplication. J Biol Chem. 270:1995;4262-4269.
-
(1995)
J Biol Chem
, vol.270
, pp. 4262-4269
-
-
Busby, R.W.1
Chang, M.D.T.2
Busby, R.C.3
Wimp, J.4
Townsend, C.A.5
-
50
-
-
0027939724
-
Exrpression in Escherichia coli of a clavaminic acid synthase isozyme-a trifunctional oxygenase involved in clavulanic acid biosynthesis
-
Lawlor EJ, Elson SW, Holland S, Cassels R, Hodgson JE, Lloyd MD, Baldwin JE, Schofield CJ. Exrpression in Escherichia coli of a clavaminic acid synthase isozyme-a trifunctional oxygenase involved in clavulanic acid biosynthesis. Tetrahedron. 50:1994;8737-8748.
-
(1994)
Tetrahedron
, vol.50
, pp. 8737-8748
-
-
Lawlor, E.J.1
Elson, S.W.2
Holland, S.3
Cassels, R.4
Hodgson, J.E.5
Lloyd, M.D.6
Baldwin, J.E.7
Schofield, C.J.8
-
51
-
-
0020488069
-
A stereochemical concept for the catalytic mechanisms of prolyl-4-hydroxylase - applicability to classification and design of inhibitors
-
Hanauskeabel HM, Gunzler V. A stereochemical concept for the catalytic mechanisms of prolyl-4-hydroxylase - applicability to classification and design of inhibitors. J Theoret Biol. 94:1982;21-455.
-
(1982)
J Theoret Biol
, vol.94
, pp. 21-455
-
-
Hanauskeabel, H.M.1
Gunzler, V.2
|