Penicillium (Jia et al. 2000) with the enzyme from Methylobacterium nodulans
strain ORS2060 showing the highest catalytic efficiency (Table 19.1). It is also
important to note that the levels of induction and expression of the acdS gene vary
according to environmental conditions and most importantly from organism to
organism.
A multiple sequence alignment of the amino acid sequence of ACC deaminase
proteins from diverse microbial origins revealed that the positions of many amino
acids are highly conserved over the course of evolution, and it has been proposed
that these specifically localized amino acids have important roles in protein functional domains (Kanika et al. 2015). PLP-dependent enzymes have been proposed to
have Tyr268, Tyr294, Lys51, and Glu295 (Pseudomonas sp. UW4 ACC deaminase
numbering scheme; Duan et al. 2013) as conserved residues at their active sites.
Several structural analysis studies of ACC deaminase including NMR and X-ray
crystallography (Karthikeyan et al. 2004) and mutagenesis, mainly for Pseudomonas
(Hontzeas et al. 2004; Ose et al. 2003) and yeast ACC deaminases (Minami et al.
1998) have shown that key residues found within the enzyme active site are Tyr269,
Tyr295, Lys51, and Glu296 (yeast ACC deaminase numbering sequence) and,
Table 19.2 (continued)
UniProt
No.
Protein name Gene name
Organism
Number of amino
acids
Q48KS9
ACCD
acdS
PSPPH_1761
Pseudomonas savastanoi 338
P30297
ACCD
acdS
Pseudomonas sp.
338
Q87YW7 ACCD
acdS
PSPTO_3675
Pseudomonas syringae
338
Q9V2L2
Putative
ACCD
PYRAB00630
Pyrococcus abyssi
330
Q8U4R3
Putative
ACCD
PF0010
Pyrococcus furiosus
329
O57809
Putative
ACCD
PH0054
Pyrococcus horikoshii
325
B2UGM5 ACCD
acdS Rpic_2004 Ralstonia pickettii
338
Q8XS35
ACCD
acdS RSp0646
Ralstonia solanacearum
338
Q93AG0 ACCD
acdS
Rhizobium
leguminosarum
339
Q9AHF0 ACCD
acdS
Rhizobium radiobacter
337
Q9URX3 Probable
ACCD
SPAC922.03
Schizosaccharomyces
pombe
338
Q9WY68 Putative
ACCD
TM_0225
Thermotoga maritima
312
Q6J256
ACCD
acdS
Variovorax paradoxus
338
C5CQC9 ACCD
acdS
Vapar_5099
Variovorax paradoxus
338
This data was extracted from the Swiss-Prot database, which was reviewed and compiled from
literature and curator-evaluated computational analysis. Here, ACC deaminase is denoted as ACCD
372
S. Ali and B. R. Glick
strain ORS2060 showing the highest catalytic efficiency (Table 19.1). It is also
important to note that the levels of induction and expression of the acdS gene vary
according to environmental conditions and most importantly from organism to
organism.
A multiple sequence alignment of the amino acid sequence of ACC deaminase
proteins from diverse microbial origins revealed that the positions of many amino
acids are highly conserved over the course of evolution, and it has been proposed
that these specifically localized amino acids have important roles in protein functional domains (Kanika et al. 2015). PLP-dependent enzymes have been proposed to
have Tyr268, Tyr294, Lys51, and Glu295 (Pseudomonas sp. UW4 ACC deaminase
numbering scheme; Duan et al. 2013) as conserved residues at their active sites.
Several structural analysis studies of ACC deaminase including NMR and X-ray
crystallography (Karthikeyan et al. 2004) and mutagenesis, mainly for Pseudomonas
(Hontzeas et al. 2004; Ose et al. 2003) and yeast ACC deaminases (Minami et al.
1998) have shown that key residues found within the enzyme active site are Tyr269,
Tyr295, Lys51, and Glu296 (yeast ACC deaminase numbering sequence) and,
Table 19.2 (continued)
UniProt
No.
Protein name Gene name
Organism
Number of amino
acids
Q48KS9
ACCD
acdS
PSPPH_1761
Pseudomonas savastanoi 338
P30297
ACCD
acdS
Pseudomonas sp.
338
Q87YW7 ACCD
acdS
PSPTO_3675
Pseudomonas syringae
338
Q9V2L2
Putative
ACCD
PYRAB00630
Pyrococcus abyssi
330
Q8U4R3
Putative
ACCD
PF0010
Pyrococcus furiosus
329
O57809
Putative
ACCD
PH0054
Pyrococcus horikoshii
325
B2UGM5 ACCD
acdS Rpic_2004 Ralstonia pickettii
338
Q8XS35
ACCD
acdS RSp0646
Ralstonia solanacearum
338
Q93AG0 ACCD
acdS
Rhizobium
leguminosarum
339
Q9AHF0 ACCD
acdS
Rhizobium radiobacter
337
Q9URX3 Probable
ACCD
SPAC922.03
Schizosaccharomyces
pombe
338
Q9WY68 Putative
ACCD
TM_0225
Thermotoga maritima
312
Q6J256
ACCD
acdS
Variovorax paradoxus
338
C5CQC9 ACCD
acdS
Vapar_5099
Variovorax paradoxus
338
This data was extracted from the Swiss-Prot database, which was reviewed and compiled from
literature and curator-evaluated computational analysis. Here, ACC deaminase is denoted as ACCD
372
S. Ali and B. R. Glick