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imb12069-sup-0001-fig_s1.docx962K

Figure S1. Multiple sequence alignment of NlYDHAD and dihydroxy-acid dehydratases of several yeast species. The amino acid sequence N. lugens (NlDHAD) is aligned with the proteins from Aspergillus niger CBS 513.88 (AnDHAD, XP_001390333), Neosartorya fischeri NRRL 181 (NfDHAD, XP_001266525) and Penicillium marneffei ATCC 18224 (PmDHAD, XP_002143860).

imb12069-sup-0002-fig_s2.docx997K

Figure S2. Multiple sequence alignment of NlYBCAT and branched-chain amino acid transaminase (BCAT) of several yeast species. The amino acid sequence N. lugens (NlBCAT) is aligned with the proteins from Aspergillus flavus NRRL3357 (AfBCAT, XP_002377249.1) and Saccharomyces cerevisiae S288c (ScBAT1 (AAB69733) and ScBAT2 (NP_012682)). The lysine residue identified as the active site of the Escherichia coli enzyme is highlighted in italics. _, * and # showed substrate-cofactor binding pocket, catalytic residue and homodimer interface on conserved domain BCAT beta family. See legend to Table 1 for further explanation.

imb12069-sup-0003-table_s1.xls44K

Table S1. Counts of enzymes identified among 521 sequences

imb12069-sup-0004-table_s2.docx26K

Table S2. Primer sequences and sizes of PCR production for reverse transcription (RT)-PCR, RACE and tissue-biased expression test in N. lugens

imb12069-sup-0005-table_s3.doc63K

Table S3. Relative synonymous codon usage values of the genes for 493 putative enzymes in the synthesis of protein amino acids

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