Note to users. If you're seeing this message, it means that your browser cannot find this page's style/presentation instructions -- or possibly that you are using a browser that does not support current Web standards. Find out more about why this message is appearing, and what you can do to make your experience of our site the best it can be.

Science 10 May 1991:
Vol. 252. no. 5007, pp. 817 - 824
DOI: 10.1126/science.2028257
Prev | Table of Contents | Next

Articles

Science, Vol 252, Issue 5007, 817-824
Copyright © 1991 by American Association for the Advancement of Science

articles

A new cofactor in a prokaryotic enzyme: tryptophan tryptophylquinone as the redox prosthetic group in methylamine dehydrogenase

WS McIntire, DE Wemmer, A Chistoserdov, and ME Lidstrom

Department of Veterans Affairs Medical Center, San Francisco, CA 94121.

Methylamine dehydrogenase (MADH), an alpha 2 beta 2 enzyme from numerous methylotrophic soil bacteria, contains a novel quinonoid redox prosthetic group that is covalently bound to its small beta subunit through two amino acyl residues. A comparison of the amino acid sequence deduced from the gene sequence of the small subunit for the enzyme from Methylobacterium extorquens AM1 with the published amino acid sequence obtained by the Edman degradation method, allowed the identification of the amino acyl constituents of the cofactor as two tryptophyl residues. This information was crucial for interpreting 1H and 13C nuclear magnetic resonance, and mass spectral data collected for the semicarbazide- and carboxymethyl-derivatized bis(tripeptidyl)-cofactor of MADH from bacterium W3A1. The cofactor is composed of two cross-linked tryptophyl residues. Although there are many possible isomers, only one is consistent with all the data: The first tryptophyl residue in the peptide sequence exists as an indole-6,7-dione, and is attached at its 4 position to the 2 position of the second, otherwise unmodified, indole side group. Contrary to earlier reports, the cofactor of MADH is not 2,7,9-tricarboxypyrroloquinoline quinone (PQQ), a derivative thereof, or pro-PQQ. This appears to be the only example of two cross-linked, modified amino acyl residues having a functional role in the active site of an enzyme, in the absence of other cofactors or metal ions.


THIS ARTICLE HAS BEEN CITED BY OTHER ARTICLES:
A catalytic di-heme bis-Fe(IV) intermediate, alternative to an Fe(IV)=O porphyrin radical.
X. Li, R. Fu, S. Lee, C. Krebs, V. L. Davidson, and A. Liu (2008)
PNAS 105, 8597-8600
   Abstract »    Full Text »    PDF »
An Oxidized Tryptophan Facilitates Copper Binding in Methylococcus capsulatus-secreted Protein MopE.
R. Helland, A. Fjellbirkeland, O. A. Karlsen, T. Ve, J. R. Lillehaug, and H. B. Jensen (2008)
J. Biol. Chem. 283, 13897-13904
   Abstract »    Full Text »    PDF »
An Activated Glutamate Residue Identified in Photosystem II at the Interface between the Manganese-stabilizing Subunit and the D2 Polypeptide.
S. Rexroth, C. C. L. Wong, J. H. Park, J. R. Yates III, and B. A. Barry (2007)
J. Biol. Chem. 282, 27802-27809
   Abstract »    Full Text »    PDF »
Involvement of a Putative [Fe-S]-cluster-binding Protein in the Biogenesis of Quinohemoprotein Amine Dehydrogenase.
K. Ono, T. Okajima, M. Tani, S. Kuroda, D. Sun, V. L. Davidson, and K. Tanizawa (2006)
J. Biol. Chem. 281, 13672-13684
   Abstract »    Full Text »    PDF »
Active Site Aspartate Residues Are Critical for Tryptophan Tryptophylquinone Biogenesis in Methylamine Dehydrogenase.
L. H. Jones, A. R. Pearson, Y. Tang, C. M. Wilmot, and V. L. Davidson (2005)
J. Biol. Chem. 280, 17392-17396
   Abstract »    Full Text »    PDF »
Use of Indirect Site-directed Mutagenesis to Alter the Substrate Specificity of Methylamine Dehydrogenase.
Y. Wang, D. Sun, and V. L. Davidson (2002)
J. Biol. Chem. 277, 4119-4122
   Abstract »    Full Text »    PDF »
Crystal Structure of Quinohemoprotein Alcohol Dehydrogenase from Comamonas testosteroni. STRUCTURAL BASIS FOR SUBSTRATE OXIDATION AND ELECTRON TRANSFER.
A. Oubrie, H. J. Rozeboom, K. H. Kalk, E. G. Huizinga, and B. W. Dijkstra (2002)
J. Biol. Chem. 277, 3727-3732
   Abstract »    Full Text »    PDF »
How many ways to craft a cofactor?.
J. P. Klinman (2001)
PNAS 98, 14766-14768
   Full Text »    PDF »
The Covalent Structure of the Small Subunit from Pseudomonas putida Amine Dehydrogenase Reveals the Presence of Three Novel Types of Internal Cross-linkages, All Involving Cysteine in a Thioether Bond.
I. Vandenberghe, J.-K. Kim, B. Devreese, A. Hacisalihoglu, H. Iwabuki, T. Okajima, S.'i. Kuroda, O. Adachi, J. A. Jongejan, J. A. Duine, et al. (2001)
J. Biol. Chem. 276, 42923-42931
   Abstract »    Full Text »    PDF »
Active-site residues are critical for the folding and stability of methylamine dehydrogenase.
D. Sun, L. H. Jones, F.S. Mathews, and V. L. Davidson (2001)
Protein Eng. Des. Sel. 14, 675-681
   Abstract »    Full Text »    PDF »
Localization of Periplasmic Redox Proteins of Alcaligenes faecalis by a Modified General Method for Fractionating Gram-Negative Bacteria.
Z. Zhu, D. Sun, and V. L. Davidson (1999)
J. Bacteriol. 181, 6540-6542
   Abstract »    Full Text »
Active-site structure of the soluble quinoprotein glucose dehydrogenase complexed with methylhydrazine: A covalent cofactor-inhibitor complex.
A. Oubrie, H. J. Rozeboom, and B. W. Dijkstra (1999)
PNAS 96, 11787-11791
   Abstract »    Full Text »    PDF »
Gated and Ungated Electron Transfer Reactions from Aromatic Amine Dehydrogenase to Azurin.
Y.-L. Hyun, Z. Zhu, and V. L. Davidson (1999)
J. Biol. Chem. 274, 29081-29086
   Abstract »    Full Text »    PDF »
Heterologous Expression of Correctly Assembled Methylamine Dehydrogenase in Rhodobacter sphaeroides.
M. E. Graichen, L. H. Jones, B. V. Sharma, R. J. M. van Spanning, J. P. Hosler, and V. L. Davidson (1999)
J. Bacteriol. 181, 4216-4222
   Abstract »    Full Text »
Crystallographic and Spectroscopic Studies of Native, Aminoquinol, and Monovalent Cation-bound Forms of Methylamine Dehydrogenase from Methylobacterium extorquens AM1.
G. Labesse, D. Ferrari, Z.-w. Chen, G.-L. Rossi, V. Kuusk, W. S. McIntire, and F. S. Mathews (1998)
J. Biol. Chem. 273, 25703-25712
   Abstract »    Full Text »    PDF »
Redox Properties of Tryptophan Tryptophylquinone Enzymes. CORRELATION WITH STRUCTURE AND REACTIVITY.
Z. Zhu and V. L. Davidson (1998)
J. Biol. Chem. 273, 14254-14260
   Abstract »    Full Text »    PDF »
A Novel Post-translational Modification Involving Bromination of Tryptophan. IDENTIFICATION OF THE RESIDUE, L-6-BROMOTRYPTOPHAN, IN PEPTIDES FROM Conus imperialis AND Conus radiatus VENOM.
A. G. Craig, E. C. Jimenez, J. Dykert, D. B. Nielsen, J. Gulyas, F. C. Abogadie, J. Porter, J. E. Rivier, L. J. Cruz, B. M. Olivera, et al. (1997)
J. Biol. Chem. 272, 4689-4698
   Abstract »    Full Text »    PDF »
Enzymatic and Electron Transfer Activities in Crystalline Protein Complexes.
A. Merli, D. E. Brodersen, B. Morini, Z.-w. Chen, R. C. E. Durley, F. S. Mathews, V. L. Davidson, and G. L. Rossi (1996)
J. Biol. Chem. 271, 9177-9180
   Abstract »    Full Text »    PDF »
Complex Formation with Methylamine Dehydrogenase Affects the Pathway of Electron Transfer from Amicyanin to Cytochrome c-551i.
V. L. Davidson and L. H. Jones (1995)
J. Biol. Chem. 270, 23941-23943
   Abstract »    Full Text »    PDF »
Spectroscopic Evidence for a Common Electron Transfer Pathway for Two Tryptophan Tryptophylquinone Enzymes.
S. L. Edwards, V. L. Davidson, Y.-L. Hyun, and P. T. Wingfield (1995)
J. Biol. Chem. 270, 4293-4298
   Abstract »    Full Text »    PDF »
Structure of an electron transfer complex: methylamine dehydrogenase, amicyanin, and cytochrome c551i.
L Chen, R. Durley, F. Mathews, and V. Davidson (1994)
Science 264, 86-90
   Abstract »    PDF »
Oxidative Modification of Tryptophan 43 in the Heme Vicinity of the F43W/H64L Myoglobin Mutant.
I. Hara, T. Ueno, S.-i. Ozaki, S. Itoh, K. Lee, N. Ueyama, and Y. Watanabe (2001)
J. Biol. Chem. 276, 36067-36070
   Abstract »    Full Text »    PDF »
Crystal Structure of Quinohemoprotein Amine Dehydrogenase from Pseudomonas putida. IDENTIFICATION OF A NOVEL QUINONE COFACTOR ENCAGED BY MULTIPLE THIOETHER CROSS-BRIDGES.
A. Satoh, J.-K. Kim, I. Miyahara, B. Devreese, I. Vandenberghe, A. Hacisalihoglu, T. Okajima, S.'i. Kuroda, O. Adachi, J. A. Duine, et al. (2002)
J. Biol. Chem. 277, 2830-2834
   Abstract »    Full Text »    PDF »
Structure of a quinohemoprotein amine dehydrogenase with an uncommon redox cofactor and highly unusual crosslinking.
S. Datta, Y. Mori, K. Takagi, K. Kawaguchi, Z.-W. Chen, T. Okajima, S.'i. Kuroda, T. Ikeda, K. Kano, K. Tanizawa, et al. (2001)
PNAS 98, 14268-14273
   Abstract »    Full Text »    PDF »


To Advertise     Find Products

Science. ISSN 0036-8075 (print), 1095-9203 (online)