Flatmark T - Search Results

1

Crystal structure of the ternary complex of the catalytic domain of human phenylalanine hydroxylase with tetrahydrobiopterin and 3-(2-thienyl)-L-alanine, and its implications for the mechanism of catalysis and substrate activation.

Andersen OA, Flatmark T, Hough E. Andersen OA, et al. Among authors: flatmark t. J Mol Biol. 2002 Jul 26;320(5):1095-108. doi: 10.1016/s0022-2836(02)00560-0. J Mol Biol. 2002. PMID: 12126628

2

2.0A resolution crystal structures of the ternary complexes of human phenylalanine hydroxylase catalytic domain with tetrahydrobiopterin and 3-(2-thienyl)-L-alanine or L-norleucine: substrate specificity and molecular motions related to substrate binding.

Andersen OA, Stokka AJ, Flatmark T, Hough E. Andersen OA, et al. Among authors: flatmark t. J Mol Biol. 2003 Oct 31;333(4):747-57. doi: 10.1016/j.jmb.2003.09.004. J Mol Biol. 2003. PMID: 14568534

3

Crystallographic analysis of the human phenylalanine hydroxylase catalytic domain with bound catechol inhibitors at 2.0 A resolution.

Erlandsen H, Flatmark T, Stevens RC, Hough E. Erlandsen H, et al. Among authors: flatmark t. Biochemistry. 1998 Nov 10;37(45):15638-46. doi: 10.1021/bi9815290. Biochemistry. 1998. PMID: 9843368

This change is consistent with a change in the ligand field symmetry of the high-spin (S = 5/2) Fe(III) from a rhombic to a nearly axial ligand field symmetry as seen upon noradrenaline binding using EPR spectroscopy [Martinez, A., Andersson, K. K., Haavik, J., and Flatmark …

This change is consistent with a change in the ligand field symmetry of the high-spin (S = 5/2) Fe(III) from a rhombic to a nearly axial lig …

4

High resolution crystal structures of the catalytic domain of human phenylalanine hydroxylase in its catalytically active Fe(II) form and binary complex with tetrahydrobiopterin.

Andersen OA, Flatmark T, Hough E. Andersen OA, et al. Among authors: flatmark t. J Mol Biol. 2001 Nov 23;314(2):279-91. doi: 10.1006/jmbi.2001.5061. J Mol Biol. 2001. PMID: 11718561

5

Deamidation of labile asparagine residues in the autoregulatory sequence of human phenylalanine hydroxylase.

Solstad T, Carvalho RN, Andersen OA, Waidelich D, Flatmark T. Solstad T, et al. Among authors: flatmark t. Eur J Biochem. 2003 Mar;270(5):929-38. doi: 10.1046/j.1432-1033.2003.03455.x. Eur J Biochem. 2003. PMID: 12603326 Free article.

Two dimensional electrophoresis has revealed a microheterogeneity in the recombinant human phenylalanine hydroxylase (hPAH) protomer, that is the result of spontaneous nonenzymatic deamidations of labile asparagine (Asn) residues [Solstad, T. and Flatmark, T. …

Two dimensional electrophoresis has revealed a microheterogeneity in the recombinant human phenylalanine hydroxylase (hPAH) protomer, that i …

6

Studies on the regulatory properties of the pterin cofactor and dopamine bound at the active site of human phenylalanine hydroxylase.

Solstad T, Stokka AJ, Andersen OA, Flatmark T. Solstad T, et al. Among authors: flatmark t. Eur J Biochem. 2003 Mar;270(5):981-90. doi: 10.1046/j.1432-1033.2003.03471.x. Eur J Biochem. 2003. PMID: 12603331 Free article.

7

Crystallization and preliminary diffraction analysis of a truncated homodimer of human phenylalanine hydroxylase.

Erlandsen H, Martinez A, Knappskog PM, Haavik J, Hough E, Flatmark T. Erlandsen H, et al. Among authors: flatmark t. FEBS Lett. 1997 Apr 7;406(1-2):171-4. doi: 10.1016/s0014-5793(97)00259-7. FEBS Lett. 1997. PMID: 9109411 Free article.

8

Crystal structure of the catalytic domain of human phenylalanine hydroxylase reveals the structural basis for phenylketonuria.

Erlandsen H, Fusetti F, Martinez A, Hough E, Flatmark T, Stevens RC. Erlandsen H, et al. Among authors: flatmark t. Nat Struct Biol. 1997 Dec;4(12):995-1000. doi: 10.1038/nsb1297-995. Nat Struct Biol. 1997. PMID: 9406548 Review.

9

Substituting Tyr¹³⁸ in the active site loop of human phenylalanine hydroxylase affects catalysis and substrate activation.

Leandro J, Stokka AJ, Teigen K, Andersen OA, Flatmark T. Leandro J, et al. Among authors: flatmark t. FEBS Open Bio. 2017 Jun 12;7(7):1026-1036. doi: 10.1002/2211-5463.12243. eCollection 2017 Jul. FEBS Open Bio. 2017. PMID: 28680815 Free PMC article.

10

Substrate-induced conformational transition in human phenylalanine hydroxylase as studied by surface plasmon resonance analyses: the effect of terminal deletions, substrate analogues and phosphorylation.

Stokka AJ, Flatmark T. Stokka AJ, et al. Among authors: flatmark t. Biochem J. 2003 Feb 1;369(Pt 3):509-18. doi: 10.1042/BJ20021009. Biochem J. 2003. PMID: 12379147 Free PMC article.

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