[1]
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NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=1459126 [NCBI, ExPASy, EBI, Israel, Japan]
van Berkel W.,
Westphal A.,
Eschrich K.,
Eppink M.,
de Kok A.;
"Substitution of Arg214 at the substrate-binding site of p-hydroxybenzoate hydroxylase from Pseudomonas fluorescens.";
Eur. J. Biochem. 210:411-419(1992).
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[2]
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PROTEIN SEQUENCE.
DOI=10.1016/0167-4838(82)90170-4; PubMed=6809053 [NCBI, ExPASy, EBI, Israel, Japan]
Weijer W.J.,
Hofsteenge J.,
Vereijken J.M.,
Jekel P.A.,
Beintema J.J.;
"Primary structure of p-hydroxybenzoate hydroxylase from Pseudomonas fluorescens.";
Biochim. Biophys. Acta 704:385-388(1982).
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[3]
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PROTEIN SEQUENCE OF 111-138 AND 270-280.
PubMed=6780352 [NCBI, ExPASy, EBI, Israel, Japan]
Hofsteenge J.,
Vereijken J.M.,
Weijer W.J.,
Beintema J.J.,
Wierenga R.K.,
Drenth J.;
"Primary and tertiary structure studies of p-hydroxybenzoate hydroxylase from Pseudomonas fluorescens. Isolation and alignment of the CNBr peptides; interactions of the protein with flavin adenine dinucleotide.";
Eur. J. Biochem. 113:141-150(1980).
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[4]
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PROTEIN SEQUENCE OF 1-52; 53-65 AND 66-110.
PubMed=6780353 [NCBI, ExPASy, EBI, Israel, Japan]
Vereijken J.M.,
Hofsteenge J.,
Bak H.J.,
Beintema J.J.;
"The amino-acid sequence of the three smallest CNBr peptides from p-hydroxybenzoate hydroxylase from Pseudomonas fluorescens.";
Eur. J. Biochem. 113:151-157(1980).
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[5]
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PROTEIN SEQUENCE OF CNBR PEPTIDES AND TERTIARY STRUCTURE.
PubMed=6406229 [NCBI, ExPASy, EBI, Israel, Japan]
Hofsteenge J.,
Weijer W.J.,
Jekel P.A.,
Beintema J.J.;
"p-hydroxybenzoate hydroxylase from Pseudomonas fluorescens. 1. Completion of the elucidation of the primary structure.";
Eur. J. Biochem. 133:91-108(1983).
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[6]
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PROTEIN SEQUENCE OF CNBR PEPTIDES AND STRUCTURE OF ACTIVE SITE.
PubMed=6406227 [NCBI, ExPASy, EBI, Israel, Japan]
Weijer W.J.,
Hofsteenge J.,
Beintema J.J.,
Wierenga R.K.,
Drenth J.;
"p-hydroxybenzoate hydroxylase from Pseudomonas fluorescens. 2. Fitting of the amino-acid sequence to the tertiary structure.";
Eur. J. Biochem. 133:109-118(1983).
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[7]
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X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
DOI=10.1016/0022-2836(79)90301-2; PubMed=40036 [NCBI, ExPASy, EBI, Israel, Japan]
Wierenga R.K.,
de Jong R.J.,
Kalk K.H.,
Hol W.G.J.,
Drenth J.;
"Crystal structure of p-hydroxybenzoate hydroxylase.";
J. Mol. Biol. 131:55-73(1979).
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[8]
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X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).
DOI=10.1016/0022-2836(88)90307-5; PubMed=3351945 [NCBI, ExPASy, EBI, Israel, Japan]
Schreuder H.A.,
van der Laan J.M.,
Hol W.G.J.,
Drenth J.;
"Crystal structure of p-hydroxybenzoate hydroxylase complexed with its reaction product 3,4-dihydroxybenzoate.";
J. Mol. Biol. 199:637-648(1988).
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[9]
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X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF REDUCED FORM.
DOI=10.1002/prot.340140205; PubMed=1409567 [NCBI, ExPASy, EBI, Israel, Japan]
Schreuder H.A.,
van der Laan J.M.,
Swarte M.B.A.,
Kalk K.H.,
Hol W.G.J.,
Drenth J.;
"Crystal structure of the reduced form of p-hydroxybenzoate hydroxylase refined at 2.3-A resolution.";
Proteins 14:178-190(1992).
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[10]
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X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF MUTANT LYS-44.
PubMed=7628466 [NCBI, ExPASy, EBI, Israel, Japan]
Eppink M.H.,
Schreuder H.A.,
van Berkel W.J.;
"Structure and function of mutant Arg44Lys of 4-hydroxybenzoate hydroxylase implications for NADPH binding.";
Eur. J. Biochem. 231:157-165(1995).
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[11]
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X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF MUTANT LYS-42 AND SER-42.
PubMed=9578477 [NCBI, ExPASy, EBI, Israel, Japan]
Eppink M.H.,
Schreuder H.A.,
van Berkel W.J.;
"Lys42 and Ser42 variants of p-hydroxybenzoate hydroxylase from Pseudomonas fluorescens reveal that Arg42 is essential for NADPH binding.";
Eur. J. Biochem. 253:194-201(1998).
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[12]
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X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF VARIANTS.
DOI=10.1016/S0014-5793(98)01726-8; PubMed=10025942 [NCBI, ExPASy, EBI, Israel, Japan]
Eppink M.H.,
Bunthol C.,
Schreuder H.A.,
van Berkel W.J.;
"Phe161 and Arg166 variants of p-hydroxybenzoate hydroxylase. Implications for NADPH recognition and structural stability.";
FEBS Lett. 443:251-255(1999).
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